Introduction and Gene Identification OpenAI o3-deep-research-2025-06-26 184 citations 2025-12-27T16:00:23.968688

Introduction and Gene Identification

Actin Filament-Associated Protein 1 (AFAP1, a.k.a. AFAP-110) is a human protein encoded by the AFAP1 gene (UniProt Q8N556) (www.ncbi.nlm.nih.gov). The gene symbol AFAP1 refers specifically to the human actin filament-associated protein 1, not to be confused with similarly named genes or transcripts in other contexts. AFAP1 was originally identified as a 110 kDa protein associated with actin filaments and as a binding partner of the Src family tyrosine kinase (www.nature.com). It is now recognized as a multi-domain adaptor protein that links signaling molecules to the actin cytoskeleton and modulates actin filament organization (www.nature.com). AFAP1 is expressed in a wide range of human tissues (low tissue specificity) and is localized intracellularly, particularly along actin filaments and at focal adhesion sites (v19.proteinatlas.org). In cell imaging, AFAP1 shows a cytosolic, granular pattern and co-localizes with actin structures including stress fibers and focal adhesions (v19.proteinatlas.org). This widespread expression suggests a general role in cytoskeletal regulation across cell types. Consistent with this, high AFAP1 levels have been observed in certain cell types (e.g. eosinophils) and tissues, indicating potential cell-specific functions in the immune and other systems (v19.proteinatlas.org) (v19.proteinatlas.org).

Protein Structure and Domains: AFAP1 is a modular protein comprising several conserved domains that underpin its function. Notably, AFAP1 contains two Pleckstrin Homology (PH) domains, an N-terminal proline-rich motif that binds SH3 domains, multiple SH2-binding motifs (tyrosine-based motifs that can bind SH2 domains when phosphorylated), a central Serine/Threonine-rich segment (substrate domain) targeted by protein kinase C (PKC), a leucine zipper motif, and a C-terminal actin-binding domain (www.nature.com) (pmc.ncbi.nlm.nih.gov). The two PH domains (often termed PH1 and PH2) suggest the protein can associate with membrane lipids or PH-domain binding proteins, and indeed PH1 at the N-terminus is implicated in binding to PKC and possibly targeting AFAP1 to specific subcellular sites (pmc.ncbi.nlm.nih.gov). The leucine zipper (LZ) near the C-terminus mediates AFAP1 self-multimerization (dimerization/oligomerization) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This multimerization, together with the actin-binding domains on each AFAP1 molecule, allows AFAP1 to function as an actin cross-linking protein, bridging actin filaments into networks or bundles (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Structural studies show that AFAP1’s LZ-driven multimer can present multiple actin-binding sites, enabling it to organize actin filaments into either loose meshworks or tightly bundled arrays depending on context (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The protein’s autoinhibitory interactions are also tied to its domain structure: in the resting state, an intramolecular contact between the N-terminal PH1 domain and the C-terminal leucine zipper keeps AFAP1 in a closed/inhibited conformation (pmc.ncbi.nlm.nih.gov). This masks its actin-crosslinking and signaling functions until appropriate signals are received. For instance, a specific single-nucleotide polymorphism (S403C) located in the second PH domain disrupts AFAP1’s normal intramolecular interactions and promotes a more open conformation, as discussed later (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In summary, AFAP1’s domain architecture is central to its function as a regulated adaptor: the PH domains and proline motifs mediate lipid and protein interactions, the leucine zipper and actin-binding domain enable scaffold formation on actin filaments, and multiple phosphorylation sites allow signal-dependent modulation of its activity (www.nature.com) (pmc.ncbi.nlm.nih.gov).

Actin Binding and Cytoskeletal Modulation

AFAP1 is classified functionally as an actin-binding and cross-linking protein that can directly bind filamentous actin (F-actin) and influence the architecture of the actin cytoskeleton (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The C-terminal ~100 amino acids of AFAP1 constitute a defined actin-binding domain that attaches to actin filaments (www.nature.com). Through its leucine zipper-driven self-association, AFAP1 can form dimers or higher-order oligomers, effectively linking actin filaments to each other. Biochemical and cell-based assays have shown that AFAP1 can organize actin filaments into different configurations: at lower concentrations or specific phosphorylation states it tends to induce looser networks, whereas under other conditions it promotes tight filament bundles (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This dynamic reflects AFAP1’s role as a cytoskeletal modulator – it is not a passive structural component, but rather an active organizer of actin filament integrity. Indeed, AFAP1 can both stabilize and remodel actin structures in response to signals. For example, in vitro experiments demonstrated that AFAP1 can cross-link actin filaments, and that this activity is enhanced by PKC-mediated phosphorylation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Protein kinase C (PKC) phosphorylates AFAP1 on its serine/threonine-rich region, and this has been shown to increase AFAP1’s actin-bundling ability (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Mechanistically, PKC phosphorylation is thought to relieve AFAP1’s autoinhibition (possibly by disrupting the PH1–leucine zipper intramolecular clamp), allowing AFAP1 to multimerize and bind actin more effectively (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). A 2002 cell biology study reported that PKC-dependent phosphorylation of AFAP1 significantly boosted its capacity to cross-link actin filaments, correlating with the formation of robust actin structures in cells (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Importantly, AFAP1’s actin-modulating function is not constitutive but is regulated by upstream signals and possibly by its own conformational state. Under basal conditions, AFAP1 appears to contribute to maintaining actin cytoskeletal support structures such as stress fibers. In highly motile breast cancer cells (MDA-MB-231), for instance, AFAP1 is required for normal stress fiber formation and actin filament cross-linking (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). Knockdown of AFAP1 in these cells led to a loss of actin stress fibers and reduced actin filament cross-linking, indicating that AFAP1 is necessary to generate the tension-bearing bundled actin architecture (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). Without AFAP1, the cells also showed decreased adhesion to the extracellular matrix (fibronectin) and an inability to form mature focal adhesions (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). Conversely, in the presence of AFAP1, cells can form robust stress fibers that transmit contractile forces to focal adhesions, promoting strong adhesion to the substrate (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). Researchers concluded that AFAP1 helps provide cytoskeletal tension through cross-linked stress fibers, which is required to stabilize focal adhesion complexes (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). This explains why AFAP1-deficient cells failed to assemble focal adhesions despite normal levels of integrins and other adhesion proteins – the actin framework needed to cluster and reinforce those adhesions was missing (www.scholars.northwestern.edu) (www.scholars.northwestern.edu).

In addition to supporting stable actin bundles, AFAP1 is also involved in the formation of dynamic actin structures like lamellipodia and podosomes under the right conditions. Studies have shown that upon certain stimuli, AFAP1 can induce actin reorganization into punctate, actin-rich structures called podosomes (or invadopodia in cancer cells) (www.nature.com) (www.nature.com). Podosomes are adhesive, actin-core structures associated with extracellular matrix degradation and cell invasion. In vascular smooth muscle cells and other cell models, activation of PKC (for example by phorbol esters) triggers rapid podosome formation, a process in which AFAP1 is a critical mediator (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). AFAP1 responds to PKC signals by altering actin filament integrity – essentially breaking down parts of stress fibers and repurposing actin into podosome cores (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). A 2004 molecular biology study by Gatesman et al. demonstrated that PKCα activates c-Src and induces podosome formation via AFAP-110 (AFAP1) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In that pathway, AFAP1 serves as a hub where PKC signals converge to locally rearrange actin and activate Src (discussed below). Notably, phosphorylation of AFAP1 has been shown to affect podosome dynamics – one report found that specific phosphorylation sites on AFAP1 control the lifespan of podosomes, influencing how long these structures persist in cells (www.nature.com). Thus, AFAP1 is instrumental in the formation and regulation of specialized invasive actin structures. Moreover, AFAP1 can also promote lamellipodia formation (broad, sheet-like actin protrusions) when its conformation is altered. Early experiments noted that certain mutations or C-terminal truncations of AFAP1 unleashed its ability to induce lamellipodia and membrane ruffles (www.nature.com). In summary, AFAP1 acts as an actin cytoskeletal regulator with a dual nature – it can stabilize actin filament bundles to support adhesion, or it can facilitate actin remodeling into structures that drive cell migration and invasion, depending on the signaling context (www.nature.com) (www.nature.com).

Adaptor Role in Src Signaling

One of AFAP1’s defining functions is serving as an adaptor protein linking signaling molecules (especially Src-family tyrosine kinases) to the actin cytoskeleton (www.ncbi.nlm.nih.gov) (www.nature.com). AFAP1 was first discovered as a binding partner and substrate of the viral Src oncoprotein (v-Src) (pmc.ncbi.nlm.nih.gov), and later work confirmed it binds the cellular Src (c-Src) and related Src-family kinases. AFAP1 contains an SH3-binding motif (PXXP) near its N-terminus that can directly bind the SH3 domain of Src (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). This interaction tethers Src in proximity to actin filaments. AFAP1 also has multiple tyrosine residues that, when phosphorylated (for instance by Src itself), create SH2-binding sites. This means AFAP1 can form a tight complex with Src by engaging both the SH3 and SH2 domains of Src (the latter upon AFAP1’s phosphorylation) (www.nature.com) (www.nature.com). Indeed, mutational studies showed that disrupting AFAP1’s SH3-binding proline motif abrogates its association with Src (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), and conversely, phosphorylation at certain YXXP motifs stabilizes the Src–AFAP1 complex (www.nature.com). Through these interactions, AFAP1 acts as a scaffold that recruits Src to actin filaments and focal adhesion sites. Functionally, this scaffolding is significant because c-Src’s activity and localization need tight regulation – c-Src in solution is auto-inhibited, but when brought to specific sites (e.g. the cell membrane or adhesions) and released from autoinhibition, it can phosphorylate targets to drive signaling pathways (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). AFAP1 has emerged as a key “Src-activating protein” that can trigger c-Src’s kinase activity in response to upstream signals (pmc.ncbi.nlm.nih.gov).

Activation of Src: Normally, c-Src is kept in a closed, inactive conformation. AFAP1 can promote Src activation by inducing a conformational change that “frees” Src from its autoinhibited state (pmc.ncbi.nlm.nih.gov). In cells stimulated with PKC or growth factors, AFAP1 is believed to undergo a conformational opening (as described earlier) and multimerize, which not only enhances actin binding but also allows AFAP1’s Src-binding motifs to engage Src more effectively (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). By binding Src’s SH3 domain, AFAP1 competes with Src’s own intramolecular SH3–linker interaction, and thus disrupts Src’s autoinhibition (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Once Src is docked on AFAP1 and released, it may phosphorylate AFAP1 further (creating SH2 docking sites), leading to a stable Src–AFAP1 complex (www.nature.com) (www.nature.com). Crucially, AFAP1-mediated Src activation has been observed in several experimental systems. For example, Clump et al. (2010) found that an inherited variant of AFAP1 (Ser403Cys) caused constitutive Src activation in cells with high Src levels (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The variant AFAP1^403C could drive Src to form active signaling structures (podosomes) without any external PKC signal, whereas wild-type AFAP1 required upstream signals to do so (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This underscores AFAP1’s normal role as a signal-responsive Src activator. Under physiological conditions, PKCα is a major upstream signal that works through AFAP1 to activate Src (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). PKC can bind AFAP1 (via the PH1 domain) and phosphorylate it (pmc.ncbi.nlm.nih.gov). Activated PKCα was shown to trigger c-Src activation and downstream podosome formation via AFAP1, meaning if AFAP1 is absent or mutated, PKC fails to fully activate Src (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Additional signaling crosstalk is involved as well – PI3K activity is required for PKC/Afap1 to activate Src, hinting that lipid products (e.g. PIP₃) or PI3K-dependent proteins (like RACK1) cooperate in this pathway (pmc.ncbi.nlm.nih.gov). AFAP1’s PH domains may bind phosphoinositides at the membrane or partner with RACK1 (Receptor for Activated C Kinase, a WD40-repeat scaffolding protein) (pmc.ncbi.nlm.nih.gov). In fact, it’s suggested that AFAP1’s PH domains help localize the PKC–AFAP–Src complex to membrane or adhesion sites, where RACK1 and lipids provide a platform (pmc.ncbi.nlm.nih.gov). Through such mechanisms, AFAP1 positions active Src in specific subcellular locales (such as focal adhesions, membrane ruffles, or podosomes) to phosphorylate target proteins and propagate signals (pmc.ncbi.nlm.nih.gov) (www.nature.com).

Biological Signaling Pathways: By linking Src to actin, AFAP1 influences multiple signal transduction pathways related to cytoskeletal dynamics and cell adhesion. Once activated by AFAP1, Src kinase can phosphorylate focal adhesion components (e.g. FAK, paxillin) and actin regulators, leading to changes in cell migration and adhesion signaling. AFAP1 thereby affects cell–ECM interaction pathways: if actin filaments are not properly organized (as in AFAP1 knockdown), focal adhesion signaling (integrin/Src/FAK signaling) is impaired (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In contrast, AFAP1’s ability to recruit Src to adhesion sites can enhance integrin-mediated signaling and focal contact turnover, facilitating dynamic movement. It is notable that AFAP1 can serve as a platform for “larger signaling complexes” (www.nature.com) – for example, an AFAP1 multimer might bring together Src, PKC, and actin filaments all in one locale, allowing crosstalk between tyrosine kinase and PKC pathways. AFAP1 has also been reported to bind other signaling or structural proteins: while AFAP1 itself does not efficiently bind cortactin (another actin-binding scaffold) (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov), its homologs do, indicating AFAP1’s binding specificity. Instead, AFAP1’s interactions seem tuned to kinases and membrane/linker proteins. In one study, AFAP1 was found to associate with p85 PI3K and facilitate localized PI3K activation in response to phorbol ester, further tying AFAP1 to the PI3K–Akt pathway (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Another study in breast cancer cells linked AFAP1 to NF-κB signaling: low molecular weight hyaluronan signals through CD44 and Toll-like receptors led to AFAP1–actin binding and an increase in MyD88-dependent NF-κB activation (www.nature.com). This suggests that AFAP1’s actin linkage can influence inflammatory signaling cascades in certain contexts. In summary, AFAP1 functions as a bridge between extracellular signals and the actin cytoskeleton, ensuring that enzymes like Src and PKC are activated at the right place and time to remodel the cytoskeleton. As an expert review summarized, AFAP1 acts as an adaptor that “brings signaling molecules to specialized signaling complexes and/or subcellular compartments, affecting the location and crosstalk between these molecules” (pmc.ncbi.nlm.nih.gov). Through this role, AFAP1 is involved in coordinating processes such as cell adhesion, migration, and invasion that require integration of signaling and cytoskeletal rearrangement (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Cellular Localization and Function in Context

Consistent with its actin-related functions, AFAP1 is predominantly an intracellular, cytoskeletal protein. High-resolution imaging and fractionation studies place AFAP1 in the cytosol and along actin filaments, with enrichment at sites of actin assembly (v19.proteinatlas.org). The Human Protein Atlas indicates AFAP1 is localized to actin filament bundles and focal adhesions in cultured human cells (v19.proteinatlas.org) (v19.proteinatlas.org). It is not a secreted protein, nor is it typically found in the nucleus; rather, it concentrates wherever actin structures and signaling molecules converge. For example, in adherent cells AFAP1 can be seen at the termini of stress fibers where they insert into focal adhesions, consistent with its role in those structures (v19.proteinatlas.org). During active cell motility, a portion of AFAP1 also redistributes to the cell periphery, colocalizing with actin in lamellipodia or forming punctate spots at invadopodia/podosomes when those are induced (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). Studies in smooth muscle cells and macrophages have visualized AFAP1 at podosome rings and cores, where it likely helps anchor the podosome’s actin bundle and connect to signaling molecules like Src (www.nature.com) (www.nature.com). The subcellular targeting of AFAP1 is at least partly directed by its PH domains binding membrane phosphoinositides, which would recruit AFAP1 to the inner plasma membrane where actin polymerization is occurring (pmc.ncbi.nlm.nih.gov). Additionally, the ability of AFAP1 to bind PKC via the PH1 domain can localize PKC (and AFAP1 with it) to specific compartments, such as the cell cortex or periphery, upon PKC activation (pmc.ncbi.nlm.nih.gov). In the unique context of differentiated cells, AFAP1’s localization hints at specialized roles – for instance, in lactating mammary epithelial cells (discussed below), AFAP1 was found to concentrate at the apical surface of milk-secreting alveolar cells in complex with active Src (www.nature.com) (www.nature.com). This apical localization suggests AFAP1 can target Src to specific membrane domains (apical vs. basal) to regulate polarized cellular functions.

Functionally, AFAP1’s presence in these locations translates to roles in several biological processes:
- Cell Adhesion: By fortifying actin stress fibers and focal adhesions, AFAP1 promotes strong cell–matrix adhesion. Loss of AFAP1 leads to defective focal contacts and reduced adhesion strength (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). AFAP1 thereby contributes to processes like cell spreading and mechanotransduction (sensing forces through focal adhesions).
- Cell Migration and Invasion: AFAP1 facilitates the dynamic rearrangement of the actin cytoskeleton needed for cell motility. It enables the formation of lamellipodia for migration and podosomes/invadopodia for invasive behavior (www.nature.com) (www.nature.com). In invasive cancer cells, AFAP1-driven actin changes can enhance cell migration through tissues.
- Signal Transduction: AFAP1’s scaffolding of Src and possibly other kinases means it helps propagate signals from integrins, growth factor receptors, and chemoattractant pathways to downstream effects like actin remodeling. It is involved in signaling cascades like Src–FAK (affecting cell movement and survival) and PKC–MAPK pathways (affecting proliferation and differentiation in some contexts) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).
- Secretory and Specialized Cellular Functions: Recent evidence suggests AFAP1 has roles in specialized cell functions that require actin remodeling. One notable example is in lactation: using an AFAP1 knockout mouse model, Ammer et al. (2014) showed that AFAP1 is required for proper milk secretion in the lactating mammary gland (www.nature.com) (www.nature.com). AFAP1-null female mice had impaired lactation characterized by accumulation of large intracellular lipid droplets and delayed secretion of milk lipids (www.nature.com). The underlying defect was tied to misregulation of c-Src – in normal lactation, prolactin hormone triggers AFAP1 to form a complex with c-Src (leading to AFAP1’s phosphorylation) and helps localize active Src to the apical side of mammary epithelial cells (www.nature.com). In the absence of AFAP1, active Src failed to localize apically and overall Src kinase activity in mammary tissue was reduced, resulting in improper signaling for milk lipid extrusion (www.nature.com) (www.nature.com). This was the first evidence of AFAP1 in a normal physiological process, and it “defined the requirement of AFAP1 for the spatial and temporal regulation of c-Src activity in the normal breast, specifically for milk production” (www.nature.com). Thus, AFAP1 can be crucial in contexts where actin-based secretion or cell shape changes are needed for function (another speculative example might be in immune cells: the Protein Atlas notes AFAP1 is elevated in eosinophils (v19.proteinatlas.org), which undergo actin-dependent degranulation and migration; it’s plausible AFAP1 contributes to those processes, though this remains to be studied).

In summary, at the cellular level AFAP1 acts at the interface of signaling and the cytoskeleton to influence a wide range of processes – from maintaining structural adhesion to enabling rapid actin reorganization for movement or secretion. By partitioning active kinases to specific sites, AFAP1 ensures that cells can swiftly reorganize their cytoskeleton in response to internal or external cues.

AFAP1 in Disease and Clinical Contexts

Given AFAP1’s central role in actin dynamics and Src signaling, it is perhaps not surprising that dysregulation of AFAP1 has been linked to cancer and other diseases. Many cancers exhibit aberrant activation of Src family kinases and cytoskeletal alterations that promote metastasis. AFAP1, as an upstream activator and scaffold of Src, often mirrors these oncogenic changes. Overexpression of AFAP1 has been observed in multiple tumor types, and it generally correlates with more aggressive disease. For example, in normal prostate epithelial cells, AFAP1 is either absent or expressed at very low levels, but in prostate carcinoma AFAP1 is significantly upregulated – with higher levels in tumors corresponding to higher Gleason grades (more advanced/aggressive cancers) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). A 2007 study by Zhang et al. found AFAP1 protein was barely detectable in benign prostate tissue but was elevated in a majority of prostate cancer specimens; the increase in AFAP1 expression tracked with tumor progression (pmc.ncbi.nlm.nih.gov). Functionally, this overexpression appears to enhance tumor cell survival and invasion: knocking down AFAP1 in prostate cancer cell lines (such as PC3) led to decreased cell proliferation, impaired cell-matrix adhesion, and reduced migration (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In mouse models of prostate cancer, AFAP1 depletion significantly inhibited tumor growth (pmc.ncbi.nlm.nih.gov). Notably, AFAP1-depleted prostate cancer cells showed defective focal adhesions and lower β1-integrin levels, consistent with the idea that AFAP1 is needed for maintaining focal contacts that allow tumor cells to adhere and signal for growth (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The same study demonstrated that re-introducing wild-type AFAP1 could rescue the aggressive traits of these cells, whereas a mutant AFAP1 unable to bind Src failed to do so (pmc.ncbi.nlm.nih.gov). Furthermore, an AFAP1 mutant lacking the PKC-interaction domain also did not restore the invasive properties, implying that both Src and PKC interactions are critical for AFAP1’s pro-tumor function in this context (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The authors concluded that AFAP1 contributes to prostate cancer progression by regulating focal contacts in a PKC-dependent manner (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

In invasive breast cancer cells (MDA-MB-231), as mentioned earlier, AFAP1 is required for stress fibers and adhesion, which might seem counterintuitive (as one might expect a metastatic cell to have fewer stress fibers). However, the ability to dynamically assemble or disassemble adhesions is key for invasion. AFAP1 provides the means to form focal adhesions (for traction) and, when signals demand, to break them down in favor of podosomes or invadopodia for matrix degradation (www.scholars.northwestern.edu) (www.scholars.northwestern.edu). Indeed, AFAP1 has been implicated in invadopodia formation and function in cancer cells. It co-localizes with actin and signaling proteins in these structures and affects their lifespan (www.nature.com). In vitro assays of invasive behavior often show that reducing AFAP1 levels impairs a cancer cell’s ability to degrade extracellular matrix, consistent with fewer or less stable invadopodia (www.nature.com). Moreover, AFAP1 interplay with integrin/Src signaling can influence epithelial–mesenchymal transition (EMT) and cell morphology in tumors (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Considering these roles, it’s not surprising that high AFAP1 expression has prognostic significance in some cancers. Data from large patient cohorts (e.g. via The Human Protein Atlas) indicate that AFAP1 mRNA levels serve as an unfavorable prognostic marker in lung cancer and renal cancer, where higher expression is associated with poorer survival (v19.proteinatlas.org) (v19.proteinatlas.org). This suggests AFAP1 could be used as part of a prognostic panel, although it’s not yet a routine clinical marker.

Another line of evidence linking AFAP1 to cancer is its coordination with Src. Src is frequently activated in cancers (but rarely mutated); instead, it’s hyper-activated by upstream signals. AFAP1 is one such upstream activator. In ovarian cancer, which often shows elevated Src activity, researchers found that AFAP1 is concomitantly upregulated. In an analysis of patient samples, over 90% of ovarian tumors showed increased AFAP1 expression alongside c-Src hyperactivity (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Furthermore, as mentioned, a significant fraction (~25%) of individuals carry a germline S403C variant in AFAP1 (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). While this variant alone is not a cancer-causing mutation, in the context of a tumor with high Src levels it can act as a “modifier”: Clump et al. (2010) reported that ovarian cancer cells with the AFAP1^403C variant activated Src and formed podosomes without the usual external PKC signal (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This means the variant AFAP1 can predispose cells to a pro-invasive, Src-active state more readily. The study proposed that this inherited variant could influence cancer progression in patients and might serve as a biomarker to predict who will respond to Src-inhibitor drugs (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In the era of precision medicine, such biomarkers are valuable; for instance, if a patient’s tumor both overexpresses Src and harbors AFAP1^403C, that tumor might be particularly dependent on the Src–AFAP1 axis and thus more sensitive to Src kinase inhibitors. This is an active area of investigation, although no specific anti-AFAP1 therapies exist yet.

Beyond cancer, AFAP1’s actin-regulatory function could be relevant to other pathologies. There is emerging interest in AFAP1’s gene locus in cardiovascular and fibrotic diseases, since actin and Src signaling modulate smooth muscle contraction and fibroblast activation. While direct studies are limited, it’s noteworthy that some omics screens have picked up dysregulation of AFAP1 or its antisense transcript in conditions like atherosclerosis and tissue fibrosis (synapse.patsnap.com). However, the clearest non-cancer role identified so far remains the lactation defect in AFAP1-knockout mice, illustrating that AFAP1 may be critical in any process requiring coordinated Src signaling and actin rearrangement (e.g. regulated secretion, immune cell activation, wound healing).

Recent Developments (2023–2024) and Future Directions

Research on AFAP1 continues to evolve, with recent studies (2021–2024) expanding our understanding of how this protein is regulated and how it impacts disease. One notable development is the recognition of AFAP1-AS1, a long non-coding RNA transcribed from the AFAP1 gene locus, which does not code for the AFAP1 protein but can influence its expression. AFAP1-AS1 has gained attention as an oncogenic lncRNA in a variety of cancers and serves as an example of how AFAP1 is embedded in a larger regulatory network. AFAP1-AS1 is frequently overexpressed in tumors (including lung, breast, gastric, and others), and high AFAP1-AS1 levels correlate with enhanced migration, invasion, and poor prognosis (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). Mechanistic studies in 2021 demonstrated that AFAP1-AS1 can act as a competing endogenous RNA (ceRNA) – specifically, it sponges microRNAs such as miR-205-5p that would otherwise suppress AFAP1 expression (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). In gastric cancer cells, silencing AFAP1-AS1 led to lowered AFAP1 protein levels and a marked decrease in cell proliferation and invasiveness, effects that could be reversed by modulating miR-205 and AFAP1 (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). This suggests that a significant part of AFAP1-AS1’s pro-tumor activity is due to upregulation of the AFAP1 protein. Consequently, AFAP1-AS1 and its controlled network (AFAP1-AS1/miR-205/AFAP1) have been proposed as therapeutic targets or biomarkers. In 2024, a comprehensive review in Current Pharmaceutical Design highlighted AFAP1-AS1’s role across gynecologic and urogenital cancers (synapse.patsnap.com), underscoring that therapies aiming to inhibit this lncRNA might indirectly curb AFAP1-driven pathways in cancer cells.

Another recent research avenue involves extracellular vesicles and circular RNAs affecting AFAP1. A 2024 study reported that an exosomal circular RNA derived from human mesenchymal stem cells can suppress cholangiocarcinoma progression by modulating a microRNA that targets AFAP1 (synapse.patsnap.com). In that study, the exosomal circRNA acted as a sponge for miR-620, relieving miR-620’s inhibition of AFAP1, thereby altering the behavior of cholangiocarcinoma cells (synapse.patsnap.com). Interestingly, in this particular context, increasing AFAP1 was associated with inhibition of tumor progression, which hints at cell-type specific roles or a complex interplay (it's possible that in cholangiocarcinoma stroma or specific subtypes, AFAP1 might exert different effects, or that the circRNA has additional targets). Nonetheless, it illustrates the current interest in the AFAP1 axis in cancer: researchers are looking not just at the protein itself, but at upstream regulators (lncRNAs, circRNAs, miRNAs) that fine-tune AFAP1 expression in disease states. These findings open the door to novel therapeutic strategies – for instance, delivering a competing oligonucleotide to soak up AFAP1-AS1, or using exosome-mediated transfer of circRNAs or miRNA mimics/inhibitors to modulate AFAP1 levels in tumors.

On the clinical research front, efforts are being made to translate knowledge of AFAP1 into clinical markers. Large-scale genomic studies in 2023 have started to identify rare variants in AFAP1 that might contribute to disease beyond cancer. For example, a 2024 precision oncology study investigating unexplained cases of familial adenomatous polyposis (FAP) – a hereditary colon cancer syndrome – utilized DNA/RNA sequencing to uncover non-APC gene contributors (synapse.patsnap.com). Intriguingly, that study (JCO Precision Oncology, May 2024) identified anomalies in AFAP1 transcripts in certain patients, suggesting that cryptic alterations in AFAP1 could underlie some cancer-predisposition in the colon (this is still a developing area, and the term “AFAP” in gastroenterology also refers to an attenuated form of polyposis, so follow-up work is needed to confirm AFAP1’s role). Nonetheless, the inclusion of AFAP1 in such cutting-edge diagnostics underscores its growing recognition.

From a therapeutic perspective, AFAP1 is not an enzyme and thus not a classic drug target, but its position at a convergence of PKC and Src pathways makes it attractive to consider in combination therapies. Src kinase inhibitors (like dasatinib) have had mixed success in solid tumors; one hypothesis is that patient stratification based on AFAP1 activity or expression could improve their efficacy. For instance, tumors with high AFAP1 (or the AFAP1^403C variant) might rely heavily on the Src-AFAP1 axis and thus be more vulnerable to Src inhibition (pmc.ncbi.nlm.nih.gov). Conversely, if AFAP1 is low, Src might be less critical or activated through alternate routes. As research moves forward, AFAP1 levels or genotype could become part of a biomarker panel to guide the use of Src inhibitors or perhaps PKC modulators. Additionally, disrupting the AFAP1–Src interaction is a conceivable strategy; some researchers have suggested designing peptides or small molecules that mask AFAP1’s SH3-binding motif or phospho-tyrosine motifs, thereby preventing it from activating Src. While still in preclinical stages, such interventions could potentially block invasive behavior in metastatic cancers with fewer side effects than broad kinase inhibitors.

In conclusion, AFAP1 (Actin Filament-Associated Protein 1) is a versatile actin-binding adaptor that plays a crucial role in connecting signal transduction to cytoskeletal remodeling. Key concepts include its domain-mediated regulation (PH domains, leucine zipper, etc.), its ability to cross-link actin filaments, and its function in activating and localizing Src family kinases. Current understanding solidifies AFAP1 as both a stabilizer of actin structures and a facilitator of dynamic actin reorganization in response to signals. Recent research (2021–2024) has shed light on the gene’s regulation by non-coding RNAs and hinted at clinical relevance in prognostics and personalized therapy. Real-world implementations are on the horizon: for example, AFAP1 is already noted as an unfavorable prognostic marker in certain cancers (v19.proteinatlas.org), and its genetic variants may inform treatment choices (pmc.ncbi.nlm.nih.gov). Expert analyses from leading studies describe AFAP1 as an essential mediator that “affects crosstalk between Src and PKC” and coordinates the assembly/disassembly of actin networks (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). As such, AFAP1 is an important node in cell biology, and continuing to unravel its interactions and regulation holds promise for understanding diseases driven by cytoskeletal dysfunction and dysregulated signaling.

References: Publications cited above include foundational studies such as Flynn et al. 1993 (AFAP1 discovery), Baisden et al. 2001 (www.nature.com), which first articulated AFAP1’s adaptor role and structure; Qian et al. 2002 (pmc.ncbi.nlm.nih.gov) on PKC phosphorylation effects; Gatesman et al. 2004 (pmc.ncbi.nlm.nih.gov) on PKC–Src–podosome signaling; Dorfleutner et al. 2007 (www.scholars.northwestern.edu) on AFAP1 in adhesion; Zhang et al. 2007 (J Clin Invest) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov) on AFAP1 in prostate cancer; Clump et al. 2010 (pmc.ncbi.nlm.nih.gov) on the AFAP1^403C variant; and Ammer et al. 2014 (www.nature.com) (www.nature.com) demonstrating AFAP1’s physiological role in mammary gland function, among others. These and more recent sources (Dang et al. 2021 (pubmed.ncbi.nlm.nih.gov), Wen et al. 2024, etc.) collectively provide a comprehensive view of AFAP1 as a critical link between cellular signals and the actin cytoskeleton, with significant implications for health and disease.

Citations

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  49. AnnotationURLCitation(end_index=15663, start_index=15535, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=,0148.%20%5BDOI%5D%20%5BPMC%20free%20article')
  50. AnnotationURLCitation(end_index=15789, start_index=15664, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=Scholar%20scholar.google.com%20%5D%20,doi')
  51. AnnotationURLCitation(end_index=16138, start_index=15951, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=%5B12%2C13%20%5D.%20In%20addition%2C%20AFAP,rich%20invasive%20structures%E2%80%94podosomes%20%5B14%2C16')
  52. AnnotationURLCitation(end_index=16337, start_index=16139, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=intermolecular%20interaction%20between%20the%20carboxy,rich%20invasive%20structures%E2%80%94podosomes%20%5B14%2C16')
  53. AnnotationURLCitation(end_index=16614, start_index=16486, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=,0148.%20%5BDOI%5D%20%5BPMC%20free%20article')
  54. AnnotationURLCitation(end_index=16751, start_index=16615, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=T%2C%20Pustula%20J%2C%20Zot%20HG%2C,Google%20Scholar')
  55. AnnotationURLCitation(end_index=17281, start_index=17123, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=ability%20to%20alter%20actin%20filament,Cell%20Res%202000%3B%20255%3A%20102%E2%80%93113')
  56. AnnotationURLCitation(end_index=17761, start_index=17669, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=motif,110%E2%80%93119')
  57. AnnotationURLCitation(end_index=18171, start_index=18032, title='The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity | Oncogene', type='url_citation', url='https://www.nature.com/articles/1204784#:~:text=as%20an%20adaptor%20protein%20by,to%20cellular%20signals%20that%20alter')
  58. AnnotationURLCitation(end_index=18319, start_index=18172, title='The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity | Oncogene', type='url_citation', url='https://www.nature.com/articles/1204784#:~:text=actin%20filament%20integrity%20that%20can,will%20review%20the%20structure%20and')
  59. AnnotationURLCitation(end_index=18646, start_index=18523, title='AFAP1 actin filament associated protein 1 [Homo sapiens (human)] - Gene - NCBI', type='url_citation', url='https://www.ncbi.nlm.nih.gov/gene/60312#:~:text=Summary%20The%20protein%20encoded%20by,Expression')
  60. AnnotationURLCitation(end_index=18786, start_index=18647, title='The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity | Oncogene', type='url_citation', url='https://www.nature.com/articles/1204784#:~:text=as%20an%20adaptor%20protein%20by,to%20cellular%20signals%20that%20alter')
  61. AnnotationURLCitation(end_index=19035, start_index=18887, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=The%20actin%20filament%E2%80%93associated%20protein%20of,binding')
  62. AnnotationURLCitation(end_index=19404, start_index=19240, title='AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/21333378/#:~:text=AFAP1L1%20is%20hypothesized%20to%20have,move%20to%20podosomes%20without%20stimulation')
  63. AnnotationURLCitation(end_index=19563, start_index=19405, title='AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/21333378/#:~:text=tyrosine%20kinase%20cSrc%20via%20an,in%20human%20tissues%20shows%20differential')
  64. AnnotationURLCitation(end_index=20024, start_index=19900, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=4,Cell%20Biochem%201997%3B%20175%3A%20243%E2%80%93252')
  65. AnnotationURLCitation(end_index=20150, start_index=20025, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=5,Mol%20Carcinogen%201998%3B%2022%3A%20110%E2%80%93119')
  66. AnnotationURLCitation(end_index=20400, start_index=20271, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,proteins%2C%20such%20as%20the%20receptor')
  67. AnnotationURLCitation(end_index=20532, start_index=20401, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,domains%20may%20potentially%20direct%20the')
  68. AnnotationURLCitation(end_index=20746, start_index=20622, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=4,Cell%20Biochem%201997%3B%20175%3A%20243%E2%80%93252')
  69. AnnotationURLCitation(end_index=21354, start_index=21181, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=Enhanced%20expression%20and%20activity%20of,presence%20of%20a%20nonsynonymous%2C%20single')
  70. AnnotationURLCitation(end_index=21517, start_index=21355, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20releases%20its%20autoinhibition,of%20input%20signals%2C%20in%20contrast')
  71. AnnotationURLCitation(end_index=21806, start_index=21644, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20releases%20its%20autoinhibition,of%20input%20signals%2C%20in%20contrast')
  72. AnnotationURLCitation(end_index=22174, start_index=22012, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20releases%20its%20autoinhibition,of%20input%20signals%2C%20in%20contrast')
  73. AnnotationURLCitation(end_index=22583, start_index=22430, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=www.ncbi.nlm.nih.gov%20%29.%20AFAP,activated%20cSrc%20to%20the%20cell')
  74. AnnotationURLCitation(end_index=22782, start_index=22584, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=intermolecular%20interaction%20between%20the%20carboxy,rich%20invasive%20structures%E2%80%94podosomes%20%5B14%2C16')
  75. AnnotationURLCitation(end_index=23087, start_index=22925, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20releases%20its%20autoinhibition,of%20input%20signals%2C%20in%20contrast')
  76. AnnotationURLCitation(end_index=23252, start_index=23088, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=activates%20cSrc%20through%20a%20direct,that%2C%20under%20conditions%20of%20cSrc')
  77. AnnotationURLCitation(end_index=23523, start_index=23399, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=4,Cell%20Biochem%201997%3B%20175%3A%20243%E2%80%93252')
  78. AnnotationURLCitation(end_index=23649, start_index=23524, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=5,Mol%20Carcinogen%201998%3B%2022%3A%20110%E2%80%93119')
  79. AnnotationURLCitation(end_index=24066, start_index=23904, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20releases%20its%20autoinhibition,of%20input%20signals%2C%20in%20contrast')
  80. AnnotationURLCitation(end_index=24202, start_index=24067, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=increase%20of%20AFAP,be%20used%20to%20predict%20the')
  81. AnnotationURLCitation(end_index=24522, start_index=24387, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=increase%20of%20AFAP,be%20used%20to%20predict%20the')
  82. AnnotationURLCitation(end_index=24681, start_index=24523, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20express%20enhanced%20levels%20of,110%20promotes%20cSrc%20activation')
  83. AnnotationURLCitation(end_index=24995, start_index=24867, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=,0148.%20%5BDOI%5D%20%5BPMC%20free%20article')
  84. AnnotationURLCitation(end_index=25156, start_index=24996, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=Scholar%20scholar.google.com%20%5D%20,directed%20activation%20of%20cSrc%20by')
  85. AnnotationURLCitation(end_index=25398, start_index=25219, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=functional%20domains%2C%20including%202%20pleckstrin,domains%20may%20potentially%20direct%20the')
  86. AnnotationURLCitation(end_index=25699, start_index=25571, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=,0148.%20%5BDOI%5D%20%5BPMC%20free%20article')
  87. AnnotationURLCitation(end_index=25836, start_index=25700, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=T%2C%20Pustula%20J%2C%20Zot%20HG%2C,Google%20Scholar')
  88. AnnotationURLCitation(end_index=26179, start_index=26058, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=doi%3A%2010.1091%2Fmbc.E01,Monoclonal')
  89. AnnotationURLCitation(end_index=26495, start_index=26338, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=association%20of%20AFAP,in%20regulating%20multiple%20cellular%20processes')
  90. AnnotationURLCitation(end_index=26814, start_index=26657, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=association%20of%20AFAP,in%20regulating%20multiple%20cellular%20processes')
  91. AnnotationURLCitation(end_index=27142, start_index=27013, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=%288%20%29.%20Both%20amino,based%20structures')
  92. AnnotationURLCitation(end_index=27288, start_index=27143, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=study%20also%20demonstrated%20that%20AFAP1,in%20the%20absence%20of%20AFAP1')
  93. AnnotationURLCitation(end_index=28031, start_index=27841, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=Disruption%20of%20actin%20organization%20abrogates,evidence%20demonstrates%20the%20multifunctional%20roles')
  94. AnnotationURLCitation(end_index=28194, start_index=28032, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=structures%20and%20disturbs%20integrin,bundling%20protein%2C%20is%20frequently')
  95. AnnotationURLCitation(end_index=28557, start_index=28443, title='The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity | Oncogene', type='url_citation', url='https://www.nature.com/articles/1204784#:~:text=AFAP,to%20alter%20actin%20filament%20integrity')
  96. AnnotationURLCitation(end_index=29053, start_index=28889, title='AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/21333378/#:~:text=AFAP1L1%20is%20hypothesized%20to%20have,move%20to%20podosomes%20without%20stimulation')
  97. AnnotationURLCitation(end_index=29212, start_index=29054, title='AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/21333378/#:~:text=tyrosine%20kinase%20cSrc%20via%20an,in%20human%20tissues%20shows%20differential')
  98. AnnotationURLCitation(end_index=29650, start_index=29529, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=doi%3A%2010.1091%2Fmbc.E01,Monoclonal')
  99. AnnotationURLCitation(end_index=29752, start_index=29651, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=,Google%20Scholar')
  100. AnnotationURLCitation(end_index=30130, start_index=29984, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=regulating%20focal%20contacts,Invest%202007%3B%20117%3A%202962%E2%80%932973')
  101. AnnotationURLCitation(end_index=30805, start_index=30676, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=%288%20%29.%20Both%20amino,based%20structures')
  102. AnnotationURLCitation(end_index=31176, start_index=30986, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=Disruption%20of%20actin%20organization%20abrogates,evidence%20demonstrates%20the%20multifunctional%20roles')
  103. AnnotationURLCitation(end_index=31339, start_index=31177, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=structures%20and%20disturbs%20integrin,bundling%20protein%2C%20is%20frequently')
  104. AnnotationURLCitation(end_index=31838, start_index=31656, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Gene%20name%5E%7Bi%7D%20AFAP1%20%28AFAP%2C%20AFAP,i%7D%20Immune%20cell%20enhanced%20%28eosinophil')
  105. AnnotationURLCitation(end_index=32149, start_index=31967, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Gene%20name%5E%7Bi%7D%20AFAP1%20%28AFAP%2C%20AFAP,i%7D%20Immune%20cell%20enhanced%20%28eosinophil')
  106. AnnotationURLCitation(end_index=32299, start_index=32150, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Subcellular%20location,actin%20filaments%20into%20both%20network')
  107. AnnotationURLCitation(end_index=32772, start_index=32623, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Subcellular%20location,actin%20filaments%20into%20both%20network')
  108. AnnotationURLCitation(end_index=33138, start_index=32986, title='AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/21333378/#:~:text=interacting%20with%20the%20SH3%20domain,brain%20where%20AFAP1%20was%20not')
  109. AnnotationURLCitation(end_index=33314, start_index=33139, title='AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/21333378/#:~:text=structures%20and%20colocalize%20with%20cortactin%2C,unique%20protein%20interactions%20in%20which')
  110. AnnotationURLCitation(end_index=33665, start_index=33515, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=binds%20to%20filamentous%20actin%20and,the%20lactating%20knockout%20mice%20were')
  111. AnnotationURLCitation(end_index=33814, start_index=33666, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=prostate%20cancer%20cells%2C%20AFAP1%20has,in%20lipid%20synthesis%20and%20the')
  112. AnnotationURLCitation(end_index=34189, start_index=34032, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=association%20of%20AFAP,in%20regulating%20multiple%20cellular%20processes')
  113. AnnotationURLCitation(end_index=34557, start_index=34378, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=functional%20domains%2C%20including%202%20pleckstrin,domains%20may%20potentially%20direct%20the')
  114. AnnotationURLCitation(end_index=34989, start_index=34844, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=study%20also%20demonstrated%20that%20AFAP1,in%20the%20absence%20of%20AFAP1')
  115. AnnotationURLCitation(end_index=35132, start_index=34990, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=activation%20in%20the%20cSrc%20knockout,in%20the%20absence%20of%20AFAP1')
  116. AnnotationURLCitation(end_index=35825, start_index=35589, title='AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells - Northwestern Scholars', type='url_citation', url='https://www.scholars.northwestern.edu/en/publications/afap-110-is-required-for-actin-stress-fiber-formation-and-cell-ad/#:~:text=approach%20confirms%20that%20MDA,231%20breast%20cancer%20cell%20adhesion')
  117. AnnotationURLCitation(end_index=36086, start_index=35826, title='AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells - Northwestern Scholars', type='url_citation', url='https://www.scholars.northwestern.edu/en/publications/afap-110-is-required-for-actin-stress-fiber-formation-and-cell-ad/#:~:text=cytoskeletal%20tension%20through%20stress%20fiber,would%20promote%20focal%20adhesion%20formation')
  118. AnnotationURLCitation(end_index=36599, start_index=36449, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=binds%20to%20filamentous%20actin%20and,the%20lactating%20knockout%20mice%20were')
  119. AnnotationURLCitation(end_index=36748, start_index=36600, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=prostate%20cancer%20cells%2C%20AFAP1%20has,in%20lipid%20synthesis%20and%20the')
  120. AnnotationURLCitation(end_index=37442, start_index=37252, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=Disruption%20of%20actin%20organization%20abrogates,evidence%20demonstrates%20the%20multifunctional%20roles')
  121. AnnotationURLCitation(end_index=37605, start_index=37443, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=structures%20and%20disturbs%20integrin,bundling%20protein%2C%20is%20frequently')
  122. AnnotationURLCitation(end_index=38079, start_index=37950, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=Actin%20filament,an%20inability%20to%20nurse%20efficiently')
  123. AnnotationURLCitation(end_index=38225, start_index=38080, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=study%20also%20demonstrated%20that%20AFAP1,in%20the%20absence%20of%20AFAP1')
  124. AnnotationURLCitation(end_index=38491, start_index=38378, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=this%20study%2C%20we%20generated%20an,This')
  125. AnnotationURLCitation(end_index=38886, start_index=38753, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=production%20of%20%CE%B2,the%20apical%20surface%20of%20luminal')
  126. AnnotationURLCitation(end_index=39217, start_index=39072, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=study%20also%20demonstrated%20that%20AFAP1,in%20the%20absence%20of%20AFAP1')
  127. AnnotationURLCitation(end_index=39374, start_index=39218, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=activation%20in%20the%20cSrc%20knockout,the%20normal%20breast%2C%20specifically%20for')
  128. AnnotationURLCitation(end_index=39766, start_index=39605, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=activation%20in%20the%20cSrc%20knockout,breast%2C%20specifically%20for%20milk%20production')
  129. AnnotationURLCitation(end_index=40175, start_index=39997, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Cancer%20prognostic%20summary%20Prognostic%20marker,actin%20filaments%20into%20both%20network')
  130. AnnotationURLCitation(end_index=41717, start_index=41553, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=affects%20crosstalk%20between%20Src%20and,110%20resulted%20in%20decreased%20cell')
  131. AnnotationURLCitation(end_index=41893, start_index=41718, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=prostatic%20hyperplasia%20but%20significantly%20increased,However%2C%20expression%20of%20an')
  132. AnnotationURLCitation(end_index=42287, start_index=42123, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=affects%20crosstalk%20between%20Src%20and,110%20resulted%20in%20decreased%20cell')
  133. AnnotationURLCitation(end_index=42690, start_index=42534, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=Downregulation%20of%20AFAP,critical%20for%20tumorigenic%20growth%2C%20in')
  134. AnnotationURLCitation(end_index=42850, start_index=42691, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=models.%20Furthermore%2C%20downmodulation%20of%20AFAP,dependent%20mechanism')
  135. AnnotationURLCitation(end_index=43120, start_index=42945, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=prostatic%20hyperplasia%20but%20significantly%20increased,However%2C%20expression%20of%20an')
  136. AnnotationURLCitation(end_index=43521, start_index=43365, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=Downregulation%20of%20AFAP,critical%20for%20tumorigenic%20growth%2C%20in')
  137. AnnotationURLCitation(end_index=43681, start_index=43522, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=models.%20Furthermore%2C%20downmodulation%20of%20AFAP,dependent%20mechanism')
  138. AnnotationURLCitation(end_index=43993, start_index=43856, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=integrin%20%CE%B21%20expression,dependent%20mechanism')
  139. AnnotationURLCitation(end_index=44346, start_index=44209, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=integrin%20%CE%B21%20expression,dependent%20mechanism')
  140. AnnotationURLCitation(end_index=44457, start_index=44347, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,dependent%20mechanism')
  141. AnnotationURLCitation(end_index=44727, start_index=44590, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=integrin%20%CE%B21%20expression,dependent%20mechanism')
  142. AnnotationURLCitation(end_index=44838, start_index=44728, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,dependent%20mechanism')
  143. AnnotationURLCitation(end_index=45564, start_index=45328, title='AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells - Northwestern Scholars', type='url_citation', url='https://www.scholars.northwestern.edu/en/publications/afap-110-is-required-for-actin-stress-fiber-formation-and-cell-ad/#:~:text=approach%20confirms%20that%20MDA,231%20breast%20cancer%20cell%20adhesion')
  144. AnnotationURLCitation(end_index=45825, start_index=45565, title='AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells - Northwestern Scholars', type='url_citation', url='https://www.scholars.northwestern.edu/en/publications/afap-110-is-required-for-actin-stress-fiber-formation-and-cell-ad/#:~:text=cytoskeletal%20tension%20through%20stress%20fiber,would%20promote%20focal%20adhesion%20formation')
  145. AnnotationURLCitation(end_index=46175, start_index=46017, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=ability%20to%20alter%20actin%20filament,Cell%20Res%202000%3B%20255%3A%20102%E2%80%93113')
  146. AnnotationURLCitation(end_index=46526, start_index=46368, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=ability%20to%20alter%20actin%20filament,Cell%20Res%202000%3B%20255%3A%20102%E2%80%93113')
  147. AnnotationURLCitation(end_index=46860, start_index=46670, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=Disruption%20of%20actin%20organization%20abrogates,evidence%20demonstrates%20the%20multifunctional%20roles')
  148. AnnotationURLCitation(end_index=47023, start_index=46861, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=structures%20and%20disturbs%20integrin,bundling%20protein%2C%20is%20frequently')
  149. AnnotationURLCitation(end_index=47528, start_index=47379, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Subcellular%20location,actin%20filaments%20into%20both%20network')
  150. AnnotationURLCitation(end_index=47710, start_index=47529, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Cancer%20prognostic%20summary%20Prognostic%20marker,Low%20human%20brain%20regional%20specificity')
  151. AnnotationURLCitation(end_index=48475, start_index=48311, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=activates%20cSrc%20through%20a%20direct,that%2C%20under%20conditions%20of%20cSrc')
  152. AnnotationURLCitation(end_index=48620, start_index=48476, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=increase%20of%20AFAP,of%20input%20signals%2C%20in%20contrast')
  153. AnnotationURLCitation(end_index=48873, start_index=48738, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=increase%20of%20AFAP,be%20used%20to%20predict%20the')
  154. AnnotationURLCitation(end_index=49022, start_index=48874, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=cSrc%20and%20the%20formation%20of,be%20used%20to%20predict%20the')
  155. AnnotationURLCitation(end_index=49457, start_index=49322, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=increase%20of%20AFAP,be%20used%20to%20predict%20the')
  156. AnnotationURLCitation(end_index=49616, start_index=49458, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=that%20express%20enhanced%20levels%20of,110%20promotes%20cSrc%20activation')
  157. AnnotationURLCitation(end_index=50056, start_index=49898, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=cSrc%20and%20the%20formation%20of,the%20response%20to%20targeted%20therapy')
  158. AnnotationURLCitation(end_index=50234, start_index=50057, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=overexpression%2C%20the%20polymorphic%20variant%20of,the%20response%20to%20targeted%20therapy')
  159. AnnotationURLCitation(end_index=51211, start_index=51066, title='AFAP1 - Drugs, Indications, Patents - Synapse', type='url_citation', url='https://synapse.patsnap.com/target/d0c14faf9cd134bcb3492bb97550290f#:~:text=Roles%20of%20AFAP1,and%20Urogenital%20System')
  160. AnnotationURLCitation(end_index=52425, start_index=52274, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=Results%3A%20qPCR%20results%20showed%20that,Luciferase%20reporter%20gene')
  161. AnnotationURLCitation(end_index=52580, start_index=52426, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=Moreover%2C%20miR,including%20proliferation%2C%20migration%20and%20invasion')
  162. AnnotationURLCitation(end_index=52954, start_index=52791, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=differentiation%20%28p%3D0,including%20proliferation%2C%20migration%20and%20invasion')
  163. AnnotationURLCitation(end_index=53109, start_index=52955, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=Moreover%2C%20miR,including%20proliferation%2C%20migration%20and%20invasion')
  164. AnnotationURLCitation(end_index=53442, start_index=53317, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=Results%3A%20qPCR%20results%20showed%20that,5p')
  165. AnnotationURLCitation(end_index=53597, start_index=53443, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=Moreover%2C%20miR,including%20proliferation%2C%20migration%20and%20invasion')
  166. AnnotationURLCitation(end_index=54141, start_index=53992, title='AFAP1 - Drugs, Indications, Patents - Synapse', type='url_citation', url='https://synapse.patsnap.com/target/d0c14faf9cd134bcb3492bb97550290f#:~:text=01%20Mar%202024Current%20pharmaceutical%20design')
  167. AnnotationURLCitation(end_index=54696, start_index=54551, title='AFAP1 - Drugs, Indications, Patents - Synapse', type='url_citation', url='https://synapse.patsnap.com/target/d0c14faf9cd134bcb3492bb97550290f#:~:text=Roles%20of%20AFAP1,and%20Urogenital%20System')
  168. AnnotationURLCitation(end_index=55013, start_index=54868, title='AFAP1 - Drugs, Indications, Patents - Synapse', type='url_citation', url='https://synapse.patsnap.com/target/d0c14faf9cd134bcb3492bb97550290f#:~:text=Roles%20of%20AFAP1,and%20Urogenital%20System')
  169. AnnotationURLCitation(end_index=56452, start_index=56310, title='AFAP1 - Drugs, Indications, Patents - Synapse', type='url_citation', url='https://synapse.patsnap.com/target/d0c14faf9cd134bcb3492bb97550290f#:~:text=01%20May%202024JCO%20precision%20oncology')
  170. AnnotationURLCitation(end_index=57678, start_index=57520, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=cSrc%20and%20the%20formation%20of,the%20response%20to%20targeted%20therapy')
  171. AnnotationURLCitation(end_index=59390, start_index=59212, title='AFAP1 protein expression summary - The Human Protein Atlas', type='url_citation', url='https://v19.proteinatlas.org/ENSG00000196526-AFAP1#:~:text=Cancer%20prognostic%20summary%20Prognostic%20marker,actin%20filaments%20into%20both%20network')
  172. AnnotationURLCitation(end_index=59604, start_index=59446, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=cSrc%20and%20the%20formation%20of,the%20response%20to%20targeted%20therapy')
  173. AnnotationURLCitation(end_index=59959, start_index=59791, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=first%20identified%20as%20a%20substrate,prostate%20cancer%20cells%20inhibited%20cell')
  174. AnnotationURLCitation(end_index=60089, start_index=59960, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,as%20phospholipids%20at%20the%20cellular')
  175. AnnotationURLCitation(end_index=60561, start_index=60447, title='The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity | Oncogene', type='url_citation', url='https://www.nature.com/articles/1204784#:~:text=AFAP,to%20alter%20actin%20filament%20integrity')
  176. AnnotationURLCitation(end_index=60802, start_index=60642, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=Scholar%20scholar.google.com%20%5D%20,directed%20activation%20of%20cSrc%20by')
  177. AnnotationURLCitation(end_index=60986, start_index=60858, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=,0148.%20%5BDOI%5D%20%5BPMC%20free%20article')
  178. AnnotationURLCitation(end_index=61221, start_index=61044, title='AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells - Northwestern Scholars', type='url_citation', url='https://www.scholars.northwestern.edu/en/publications/afap-110-is-required-for-actin-stress-fiber-formation-and-cell-ad/#:~:text=AFAP,Although')
  179. AnnotationURLCitation(end_index=61403, start_index=61280, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,motifs%20are%20involved%20in%20the')
  180. AnnotationURLCitation(end_index=61533, start_index=61404, title='AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1978423/#:~:text=AFAP,proteins%2C%20such%20as%20the%20receptor')
  181. AnnotationURLCitation(end_index=61747, start_index=61583, title='A Polymorphic Variant of AFAP-110 Enhances cSrc Activity - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2915419/#:~:text=activates%20cSrc%20through%20a%20direct,that%2C%20under%20conditions%20of%20cSrc')
  182. AnnotationURLCitation(end_index=61944, start_index=61799, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=study%20also%20demonstrated%20that%20AFAP1,in%20the%20absence%20of%20AFAP1')
  183. AnnotationURLCitation(end_index=62101, start_index=61945, title='Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland | Oncogene', type='url_citation', url='https://www.nature.com/articles/onc2014205#:~:text=activation%20in%20the%20cSrc%20knockout,the%20normal%20breast%2C%20specifically%20for')
  184. AnnotationURLCitation(end_index=62397, start_index=62234, title='LncRNA AFAP1-AS1 Modulates the Proliferation and Invasion of Gastric Cancer Cells by Regulating AFAP1 via miR-205-5p - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34234560/#:~:text=differentiation%20%28p%3D0,including%20proliferation%2C%20migration%20and%20invasion')