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CD2AP (CD2-associated protein, UniProt Q9Y5K6) is a human gene encoding a 639-amino acid multifunctional scaffolding and adapter protein (mehrabipour2023asystematiccompilation pages 1-2, zhang2024cd2appromotesthe pages 1-2). The protein is characterized by three consecutive SH3 (Src Homology 3) domains and proline-rich regions, which mediate diverse protein-protein interactions (mehrabipour2023asystematiccompilation pages 1-2, arden2024themyo1finteractome pages 1-3). CD2AP was initially identified as an SH3-containing protein that binds to the CD2 receptor via its cytoplasmic domain (fitzsimons2024cd2apiscoexpressed pages 1-3).
Core Adapter/Scaffold Function
CD2AP functions primarily as a scaffolding/adapter protein that coordinates protein-protein interactions through its structural domains (zhang2024cd2appromotesthe pages 1-2, ha2013rolesofadaptor pages 1-2). The three SH3 domains recognize and bind proline-rich motifs (PxxP consensus sequences) in partner proteins, enabling CD2AP to assemble multiprotein complexes (mehrabipour2023asystematiccompilation pages 1-2). This modular architecture allows CD2AP to serve as a hub where signaling pathway components converge, and when the required combination of interactions are formed, corresponding downstream signaling cascades are activated (fitzsimons2024cd2apiscoexpressed pages 1-3).
Binding Specificity and Partner Proteins
The SH3 domains of CD2AP mediate multivalent proline-rich motif interactions with numerous binding partners (arden2024themyo1finteractome pages 1-3, mehrabipour2023asystematiccompilation pages 1-2). Recent proximity labeling studies identified a distinct SH3-domain-dependent adaptor module comprising CD2AP, ASAP1, SH3BP2, and SH3KBP1, termed the CASS group of proteins (arden2024themyo1finteractome pages 1-3, arden2024themyo1finteractome pages 3-6). These interactions involve structural modeling-confirmed multivalent binding between proline-rich motifs in partner proteins and the MYO1F SH3 domain, which also associates with CD2AP (arden2024themyo1finteractome pages 1-3).
A comprehensive summary of CD2AP binding partners and their functional roles is provided below:
| Binding Partner | Interaction Domain (on CD2AP) | Cellular Context/Location | Functional Role |
|---|---|---|---|
| Nephrin | Primarily C-terminal/adaptor interface; CD2AP functions as a scaffold linking nephrin to downstream cytoskeletal machinery | Podocyte slit diaphragm, lipid raft-associated junctional complex | Couples slit-diaphragm signaling to actin remodeling; helps maintain foot-process architecture and filtration barrier integrity (blaine2020regulationofthe pages 3-5, ha2013rolesofadaptor pages 1-2, swiateckaurban2017endocytictraffickingat pages 1-2) |
| Podocin | C-terminal region of podocin binds CD2AP scaffold; exact CD2AP subsite not fully resolved in these sources | Podocyte slit diaphragm/lipid rafts | Stabilizes the nephrin–podocin–CD2AP complex and links slit-diaphragm components to the actin cytoskeleton (blaine2020regulationofthe pages 3-5, ha2013rolesofadaptor pages 1-2, swiateckaurban2017endocytictraffickingat pages 1-2) |
| F-actin / actin cytoskeleton | Direct/functional actin-associating regions outside the SH3 cluster; CD2AP also links actin indirectly through partner proteins | Podocyte foot processes, vesicles, cortical cytoskeleton, phagocytic structures | Structural linkage between membrane complexes and actin; supports cytoskeletal organization, vesicle trafficking, and cell shape control (blaine2020regulationofthe pages 3-5, tolvanen2015lackofcd2ap pages 1-4, zhang2024cd2appromotesthe pages 1-2) |
| TrkA | Scaffold interface enabling assembly of receptor-signaling complexes; specific residue-level site not defined here | Neurons, especially NGF-responsive sensory and basal forebrain cholinergic neurons | Coordinates NGF-dependent trophic signaling and receptor-linked retrograde signaling/endocytosis (fitzsimons2024cd2apiscoexpressed pages 1-3) |
| Rab5 | Endosomal/scaffold association; specific CD2AP subdomain not defined here | Rab5-positive endosomes in neurons; endocytic compartments | Supports Rab5-mediated endocytosis and retrograde transport/signaling from internalized receptor complexes (fitzsimons2024cd2apiscoexpressed pages 1-3) |
| PI3K p85 | Scaffold-binding interface assembling signaling complexes downstream of receptors | Neurons; also broader signaling complexes | Promotes PI3K/Akt pathway coupling downstream of trophic receptors such as TrkA (fitzsimons2024cd2apiscoexpressed pages 1-3) |
| Clathrin | Complex formation with CD2AP; likely via non-SH3 scaffold regions coordinating vesicle machinery | Perinuclear region, clathrin-coated/recycling vesicles, podocytes | Connects clathrin to actin and supports vesicle sorting/recycling, including Glut4 trafficking (tolvanen2015lackofcd2ap pages 1-4) |
| Cortactin | Direct/functional interaction outside core SH3 ligand-binding description in these sources | Podocyte actin cytoskeleton/slit diaphragm-associated actin network | Reinforces the link from nephrin/CD2AP complexes to actin assembly and cytoskeletal remodeling (blaine2020regulationofthe pages 3-5) |
| Synaptopodin | Direct/functional interaction; exact subdomain not specified here | Podocyte foot processes and actin-rich structures | Helps connect slit-diaphragm signaling to actin bundle organization and podocyte structural stability (blaine2020regulationofthe pages 3-5) |
| ASAP1 | SH3-domain-dependent interaction, involving proline-rich motif recognition | Macrophage and microglial podosomes; MYO1F-associated adaptor module | Adaptor in podosomes/phagocytic structures; implicated in actin-rich adhesion and membrane-remodeling complexes (arden2024themyo1finteractome pages 3-6, arden2024themyo1finteractome pages 1-3) |
| SH3BP2 | SH3-domain-dependent interaction, involving proline-rich motif recognition | Immune cells; MYO1F-associated adaptor module | Participates in MYO1F-associated adaptor network in podosomes/phagocytic cups (arden2024themyo1finteractome pages 3-6, arden2024themyo1finteractome pages 1-3) |
| SH3KBP1 (CIN85) | SH3-domain-dependent interaction, involving proline-rich motif recognition | Immune cells; podocytes; phagocytic cups | Component of the CASS adaptor module; linked to endocytosis, actin regulation, and phagocytic structures (arden2024themyo1finteractome pages 3-6, swiateckaurban2017endocytictraffickingat pages 2-3) |
| GGA2 | Complex formation with CD2AP; specific CD2AP site not resolved here | Podocyte trans-Golgi/GSV trafficking pathway | Sorts Glut4 toward storage vesicles and supports insulin-responsive glucose transporter trafficking (tolvanen2015lackofcd2ap pages 1-4) |
| TRIM5 | Interaction site not mapped in the retrieved context | Glioblastoma cells | Stabilizes/promotes TRIM5-associated NF-κB signaling, enhancing malignant phenotypes in GBM models (zhang2024cd2appromotesthe pages 1-2) |
Table: This table summarizes major experimentally discussed CD2AP interaction partners, the CD2AP region implicated where available, the cellular context, and the functional consequence of each interaction. It is useful for linking CD2AP's scaffold architecture to specific pathways in podocytes, neurons, immune cells, and cancer.
CD2AP exhibits cell type-specific subcellular localization patterns that reflect its diverse functional roles (arden2024themyo1finteractome pages 3-6, blaine2020regulationofthe pages 3-5, fitzsimons2024cd2apiscoexpressed pages 1-3):
| Cell Type | Subcellular Location | Key Associated Proteins at that Location | Functional Significance |
|---|---|---|---|
| Podocytes | Slit diaphragm at foot processes; lipid raft-associated junctional complex | Nephrin, podocin, Neph1, ZO-1, actin/cortical cytoskeleton | Links slit-diaphragm receptors to the actin cytoskeleton, helping maintain foot-process architecture, filtration barrier integrity, and slit-diaphragm signaling (blaine2020regulationofthe pages 3-5, ha2013rolesofadaptor pages 1-2, swiateckaurban2017endocytictraffickingat pages 1-2) |
| Podocytes | Endocytic vesicles and endosomal/lysosomal compartments; perinuclear trafficking region | Clathrin, GGA2, Glut4, IRAP, sortilin, Rab5 | Supports endosomal sorting, vesicle recycling, and cargo trafficking, including insulin-responsive Glut4 trafficking and nephrin/podocin turnover (tolvanen2015lackofcd2ap pages 1-4, swiateckaurban2017endocytictraffickingat pages 2-3, tian2022podocyteendocytosisin pages 1-2) |
| Podocytes | Focal adhesion- and actin-associated regions in foot processes | F-actin, cortactin, synaptopodin, α-actinin-4 | Couples junctional and membrane signals to actin remodeling, podocyte shape control, and structural stability under mechanical stress (blaine2020regulationofthe pages 3-5, blaine2020regulationofthe pages 1-3) |
| Neurons (general/adult brain) | Pre-synaptic terminals and neuronal processes | Synaptic proteostasis-related proteins; endocytic machinery | Recent work indicates CD2AP contributes to neuronal structure, synaptic homeostasis, and plasticity; presynaptic localization is consistent with a role in trafficking/signaling at nerve terminals (fitzsimons2024cd2apiscoexpressed pages 1-3) |
| Basal forebrain cholinergic neurons | Soma and cholinergic projections; Rab5-decorated endosomes | Rab5, TrkA, PI3K p85 | Enriched in NGF-responsive cholinergic neurons, where it is positioned to coordinate retrograde trophic signaling and Rab5-mediated endocytosis relevant to neuronal maintenance and Alzheimer’s disease biology (fitzsimons2024cd2apiscoexpressed pages 1-3) |
| Immune cells (macrophages, microglia) | Podosomes | MYO1F, ASAP1, SH3BP2, SH3KBP1 | Colocalization in actin-rich podosomes supports a role in adhesion, membrane remodeling, and actin-dependent immune cell motility/function (arden2024themyo1finteractome pages 3-6, arden2024themyo1finteractome pages 1-3) |
| Immune cells (macrophages, microglia) | Phagocytic cups | MYO1F, SH3KBP1, ASAP1 | Localization at phagocytic cups indicates participation in phagocytosis-related membrane–cytoskeleton coupling and cup dynamics, especially in myeloid cells and disease-associated microglia (arden2024themyo1finteractome pages 3-6, arden2024themyo1finteractome pages 1-3) |
| General endocytic compartments across cell types | Plasma membrane-associated endocytic sites, clathrin-linked vesicles, Rab5-positive early endosomes, late endosomal compartments | Clathrin, Rab5, receptor cargoes, actin network components | CD2AP broadly functions at membrane-trafficking interfaces to connect cargo sorting and receptor internalization with actin remodeling and downstream signaling outputs (tolvanen2015lackofcd2ap pages 1-4, fitzsimons2024cd2apiscoexpressed pages 1-3, tian2022podocyteendocytosisin pages 1-2) |
Table: This table summarizes where CD2AP localizes in major relevant human cell contexts and what proteins and functions are associated with each location. It is useful for linking CD2AP’s scaffold role to specific subcellular compartments and biological processes.
Podocytes: CD2AP localizes prominently to the slit diaphragm, a specialized intercellular junction connecting foot processes of glomerular podocytes (ha2013rolesofadaptor pages 1-2, blaine2020regulationofthe pages 3-5, swiateckaurban2017endocytictraffickingat pages 1-2). At this location, CD2AP is found in lipid raft-associated junctional complexes together with nephrin, podocin, and Neph1 (blaine2020regulationofthe pages 3-5, swiateckaurban2017endocytictraffickingat pages 2-3). CD2AP also associates with endocytic vesicles and endosomal/lysosomal compartments in podocytes, where it participates in vesicle trafficking and receptor turnover (tolvanen2015lackofcd2ap pages 1-4, tian2022podocyteendocytosisin pages 1-2, swiateckaurban2017endocytictraffickingat pages 2-3).
Neurons: In the central nervous system, CD2AP protein is broadly expressed in adult mouse brain, including cortical and hippocampal neurons, where it is detected at pre-synaptic terminals (mehrabipour2023asystematiccompilation pages 1-2). CD2AP mRNA and protein are particularly enriched in TrkA-expressing cholinergic neurons of the adult basal forebrain, where the protein co-localizes with RAB5-decorated endosomes in neuronal soma (fitzsimons2024cd2apiscoexpressed pages 1-3). This localization suggests a role in retrograde trophic signaling in NGF-responsive CNS cholinergic neurons (fitzsimons2024cd2apiscoexpressed pages 1-3).
Immune Cells: Immunofluorescence revealed co-localization of CD2AP with MYO1F and the CASS group of proteins at actin-rich podosomes and phagocytic cups in macrophages and microglia (arden2024themyo1finteractome pages 1-3, arden2024themyo1finteractome pages 3-6). CD2AP is also expressed in migratory dendritic cell populations (fitzsimons2024cd2apiscoexpressed pages 1-3).
1. Slit Diaphragm-Actin Cytoskeleton Coupling
CD2AP plays a critical structural and signaling role at the podocyte slit diaphragm by linking transmembrane proteins to the actin cytoskeleton (ha2013rolesofadaptor pages 1-2, blaine2020regulationofthe pages 3-5, blaine2020regulationofthe pages 1-3). CD2AP functions as an adapter protein that anchors slit diaphragm proteins (nephrin, podocin) to actin filaments of podocyte foot processes (agarwal2021renalcellmarkers pages 1-2). The nephrin-podocin-CD2AP complex provides a direct link between the signal receptor nephrin and the foot process actin cytoskeleton, as CD2AP can interact directly with F-actin as well as with cortactin and synaptopodin (blaine2020regulationofthe pages 3-5, blaine2020regulationofthe pages 1-3).
CD2AP interacts with the C-terminus of podocin and helps stabilize the nephrin-podocin complex at lipid rafts within the slit diaphragm membranes (blaine2020regulationofthe pages 3-5, swiateckaurban2017endocytictraffickingat pages 2-3). This complex is essential for maintaining foot process architecture and glomerular filtration barrier integrity (ha2013rolesofadaptor pages 1-2, yu2018proteinurickidneydiseases pages 1-2). Genetic deletion or loss of CD2AP function results in foot process effacement, defective slit diaphragm formation, and proteinuria, ultimately leading to renal failure in mice (tolvanen2015lackofcd2ap pages 1-4, blaine2020regulationofthe pages 1-3).
2. Endocytic Trafficking and Vesicle Sorting
CD2AP participates in multiple endocytic pathways, including clathrin-mediated endocytosis and clathrin-independent mechanisms (tolvanen2015lackofcd2ap pages 1-4, tian2022podocyteendocytosisin pages 1-2, swiateckaurban2017endocytictraffickingat pages 2-3). CD2AP co-localizes with COPI vesicles and clathrin and has been shown to link clathrin to the actin cytoskeleton (tolvanen2015lackofcd2ap pages 1-4). CD2AP forms a complex with the clathrin adaptor GGA2, which sorts Glut4 to Glut4 storage vesicles (GSVs) in podocytes (tolvanen2015lackofcd2ap pages 1-4).
In the absence of CD2AP, clathrin recycling back to trans-Golgi membranes from the vesicular fraction containing GSVs is defective, leading to reduced insulin-stimulated trafficking of GSVs and attenuated glucose uptake (tolvanen2015lackofcd2ap pages 1-4). CD2AP also co-fractionates with Glut4, IRAP, and sortilin, constituents of Glut4 storage vesicles, and regulates insulin-dependent glucose transporter 4 (Glut4) trafficking (tolvanen2015lackofcd2ap pages 1-4).
CD2AP is present in specific late endosomal compartments in podocytes and is involved in endosomal sorting and/or trafficking by regulating the assembly of actin on vesicles (tolvanen2015lackofcd2ap pages 1-4). The protein associates with the active form of small GTPase Rab4 and Rab5, both involved in endocytic processes (tolvanen2015lackofcd2ap pages 1-4, fitzsimons2024cd2apiscoexpressed pages 1-3).
3. Neuronal Trophic Signaling
In neurons, CD2AP functions as a docking-scaffold/adaptor protein coordinator of nerve growth factor (NGF) trophic signaling and RAB5-mediated endocytosis (fitzsimons2024cd2apiscoexpressed pages 1-3). Known upstream binding-partners include Tropomyosin receptor kinase-A (TrkA), activated by NGF, while downstream effector binding-partners include the PI3K regulatory subunit p85, p21ras, and Akt (fitzsimons2024cd2apiscoexpressed pages 1-3).
NGF stimulates CD2AP binding to TrkA and the PI3-kinase effector (p85) to upregulate the PI3K/AKT pathway, functioning as a positive coordinator of NGF-stimulated axon growth and branching (fitzsimons2024cd2apiscoexpressed pages 1-3). CD2AP scaffolding interactions regulate Rab5-mediated endocytosis, which is critical for retrograde trophic signaling through endosomal transport of internalized ligand-receptor complexes towards downstream effectors located in the cell body (fitzsimons2024cd2apiscoexpressed pages 1-3).
Recent studies demonstrate that deletion of Cd2ap altered dendritic branching and spine density, impaired ubiquitin-proteasome system activity, and resulted in increased paired-pulse facilitation at hippocampal Schaffer-collateral synapses, consistent with a haploinsufficient requirement for pre-synaptic release (mehrabipour2023asystematiccompilation pages 1-2). These findings reveal conserved, dose-sensitive requirements for CD2AP in the maintenance of neuronal structure and function, including synaptic homeostasis and plasticity (mehrabipour2023asystematiccompilation pages 1-2).
4. Podosomes and Phagocytosis
CD2AP, identified as a novel adaptor protein in podosomes and phagosomes, co-localizes with MYO1F at actin-rich podosomes and phagocytic cups in macrophages and microglia (arden2024themyo1finteractome pages 1-3, arden2024themyo1finteractome pages 3-6). Functional assays demonstrated that MYO1F recruitment to the phagocytic cup requires intact SH3 domains, which interact with the CASS group of adaptor proteins including CD2AP (arden2024themyo1finteractome pages 1-3). This work offers new insights into MYO1F function in disease-associated microglia during neurodegeneration, as CD2AP is an Alzheimer's disease (AD) risk gene upregulated in microglia of individuals with AD (arden2024themyo1finteractome pages 1-3).
5. Additional Signaling Pathways
CD2AP has been reported to interact with TRIM5, an NF-κB modulator, in glioblastoma cells (zhang2024cd2appromotesthe pages 1-2). CD2AP overexpression increased TRIM5 levels and NF-κB activity, while CD2AP knockdown had the opposite effects (zhang2024cd2appromotesthe pages 1-2). This CD2AP-TRIM5-NF-κB axis promotes glioblastoma progression through activating NF-κB signaling (zhang2024cd2appromotesthe pages 1-2).
In cultured podocytes, OCRL (an inositol 5-phosphatase) associated with the linker protein IPIP27A and CD2AP, a protein important for maintenance of the podocyte slit diaphragm (preston2020arolefor pages 1-2). CD2AP is also important in the regulation of endocytic trafficking, which requires endosomal trafficking and actin polymerization (preston2020arolefor pages 1-2).
Alzheimer's Disease: Genome-wide association studies (GWAS) with multiple human populations have identified single nucleotide variants of the CD2AP gene locus associated with Alzheimer's Disease (AD) risk (fitzsimons2024cd2apiscoexpressed pages 1-3, arden2024themyo1finteractome pages 1-3, mehrabipour2023asystematiccompilation pages 1-2). CD2AP is robustly expressed in non-neuronal cells and neurovasculature in the adult CNS, with restricted neuronal expression enriched in cholinergic neurons of the basal forebrain that project to the hippocampus and cortex and are required for learning and memory (fitzsimons2024cd2apiscoexpressed pages 1-3). Basal forebrain cholinergic neurons are critical for brain health during aging, and disruption of RAB5-mediated endocytosis in these neurons is central to AD pathogenesis (fitzsimons2024cd2apiscoexpressed pages 1-3).
A 2024 study demonstrated that CD2AP is a dose-sensitive determinant of synaptic structure and plasticity (mehrabipour2023asystematiccompilation pages 1-2). Cd2ap heterozygous mice demonstrated subtle impairments in discrimination learning, and based on unbiased proteomics, partial or complete loss of Cd2ap triggered perturbation of proteins with roles in protein folding, lipid metabolism, proteostasis, and synaptic function (mehrabipour2023asystematiccompilation pages 1-2).
Immune Function: CD2AP was identified in 2024 as a novel adaptor protein in podosomes and during phagocytosis, offering new insights into its function in disease-associated microglia during neurodegeneration (arden2024themyo1finteractome pages 1-3). Interestingly, CD2AP is an AD risk gene upregulated in patient microglia implicated in phagocytic responses to amyloid-β (arden2024themyo1finteractome pages 1-3).
The functional characterization of CD2AP has employed diverse experimental approaches across multiple model systems:
Genetic models: CD2AP knockout mice die at 6 weeks due to renal failure with defective slit diaphragm formation (tolvanen2015lackofcd2ap pages 1-4, blaine2020regulationofthe pages 1-3). Conditional Cd2ap knockout and haploinsufficient mouse models have revealed dose-sensitive requirements for neuronal function (mehrabipour2023asystematiccompilation pages 1-2).
Structural studies: Structural modeling and mutagenesis confirmed multivalent proline-rich motif interactions between partner proteins and CD2AP SH3 domains (arden2024themyo1finteractome pages 1-3, mehrabipour2023asystematiccompilation pages 1-2).
Proximity labeling proteomics: In situ proximity labeling using BioID in human myeloid cells defined the MYO1F interactome and identified the SH3-domain-dependent CASS adaptor module (arden2024themyo1finteractome pages 1-3, arden2024themyo1finteractome pages 3-6).
Cell biology: Immunofluorescence, live cell imaging, subcellular fractionation, and co-immunoprecipitation studies have mapped CD2AP localization and binding partners across multiple cell types (arden2024themyo1finteractome pages 1-3, tolvanen2015lackofcd2ap pages 1-4, fitzsimons2024cd2apiscoexpressed pages 1-3, preston2020arolefor pages 1-2).
Functional assays: Studies have assessed glucose uptake, vesicle trafficking, synaptic transmission, phagocytosis, and podocyte foot process dynamics to define CD2AP functional roles (tolvanen2015lackofcd2ap pages 1-4, mehrabipour2023asystematiccompilation pages 1-2, arden2024themyo1finteractome pages 1-3).
CD2AP is a multifunctional scaffolding/adapter protein with three consecutive SH3 domains that mediate specific protein-protein interactions with diverse partners across multiple cell types. The primary molecular function of CD2AP is to link membrane receptors and junctional proteins to the actin cytoskeleton while coordinating endocytic trafficking and signaling pathways. In podocytes, CD2AP is essential for maintaining the slit diaphragm-actin connection that preserves glomerular filtration barrier integrity. In neurons, CD2AP coordinates trophic signaling and retrograde transport critical for synaptic function and neuronal maintenance. In immune cells, CD2AP participates in podosome and phagocytic cup dynamics. The protein's involvement in endocytosis, actin regulation, and signaling integration positions CD2AP as a critical node in cellular homeostasis, with implications for kidney disease, neurodegeneration, and immune function.
References
(mehrabipour2023asystematiccompilation pages 1-2): Mehrnaz Mehrabipour, Neda S. Kazemein Jasemi, Radovan Dvorsky, and Mohammad R. Ahmadian. A systematic compilation of human sh3 domains: a versatile superfamily in cellular signaling. Cells, 12:2054, Aug 2023. URL: https://doi.org/10.3390/cells12162054, doi:10.3390/cells12162054. This article has 50 citations.
(zhang2024cd2appromotesthe pages 1-2): Liang Zhang, Jiawei He, Wentao Zhao, Yuhang Zhou, Jin Li, Shaobo Li, Wenpeng Zhao, Lingliang Zhang, Ziqian Tang, Guowei Tan, Sifang Chen, Bingchang Zhang, Yun-wu Zhang, and Zhanxiang Wang. Cd2ap promotes the progression of glioblastoma multiforme via trim5-mediated nf-kb signaling. Cell Death & Disease, Oct 2024. URL: https://doi.org/10.1038/s41419-024-07094-7, doi:10.1038/s41419-024-07094-7. This article has 21 citations and is from a peer-reviewed journal.
(arden2024themyo1finteractome pages 1-3): Susan D. Arden, Eva Pennink, András Lakatos, Gillian M. Griffiths, Anna H. Lippert, and Folma Buss. The myo1f interactome reveals asap1, cd2ap and sh3kbp1 as novel adaptor proteins in podosomes and phagosomes. Journal of Cell Science, Dec 2024. URL: https://doi.org/10.1242/jcs.264357, doi:10.1242/jcs.264357. This article has 1 citations and is from a domain leading peer-reviewed journal.
(fitzsimons2024cd2apiscoexpressed pages 1-3): Lindsey Avery Fitzsimons, Mohammad Atif-Sheikh, Jayden Lovely, Madison Mueth, Makaela Rice, Kevin Kotredes, Gareth Howell, and Benjamin J Harrison. Cd2ap is co-expressed with tropomyosin-related kinase a and ras-related protein rab-5a in cholinergic neurons of the murine basal forebrain. bioRxiv, Jul 2024. URL: https://doi.org/10.1101/2024.07.24.604961, doi:10.1101/2024.07.24.604961. This article has 1 citations.
(ha2013rolesofadaptor pages 1-2): Tae-Sun Ha. Roles of adaptor proteins in podocyte biology. World journal of nephrology, 2 1:1-10, Feb 2013. URL: https://doi.org/10.5527/wjn.v2.i1.1, doi:10.5527/wjn.v2.i1.1. This article has 61 citations.
(arden2024themyo1finteractome pages 3-6): Susan D. Arden, Eva Pennink, András Lakatos, Gillian M. Griffiths, Anna H. Lippert, and Folma Buss. The myo1f interactome reveals asap1, cd2ap and sh3kbp1 as novel adaptor proteins in podosomes and phagosomes. Journal of Cell Science, Dec 2024. URL: https://doi.org/10.1242/jcs.264357, doi:10.1242/jcs.264357. This article has 1 citations and is from a domain leading peer-reviewed journal.
(blaine2020regulationofthe pages 3-5): Judith Blaine and James Dylewski. Regulation of the actin cytoskeleton in podocytes. Cells, 9:1700, Jul 2020. URL: https://doi.org/10.3390/cells9071700, doi:10.3390/cells9071700. This article has 180 citations.
(swiateckaurban2017endocytictraffickingat pages 1-2): Agnieszka Swiatecka-Urban. Endocytic trafficking at the mature podocyte slit diaphragm. Frontiers in Pediatrics, Feb 2017. URL: https://doi.org/10.3389/fped.2017.00032, doi:10.3389/fped.2017.00032. This article has 35 citations.
(tolvanen2015lackofcd2ap pages 1-4): Tuomas A. Tolvanen, Surjya Narayan Dash, Zydrune Polianskyte-Prause, Vincent Dumont, and Sanna Lehtonen. Lack of cd2ap disrupts glut4 trafficking and attenuates glucose uptake in podocytes. Journal of Cell Science, 128:4588-4600, Dec 2015. URL: https://doi.org/10.1242/jcs.175075, doi:10.1242/jcs.175075. This article has 21 citations and is from a domain leading peer-reviewed journal.
(swiateckaurban2017endocytictraffickingat pages 2-3): Agnieszka Swiatecka-Urban. Endocytic trafficking at the mature podocyte slit diaphragm. Frontiers in Pediatrics, Feb 2017. URL: https://doi.org/10.3389/fped.2017.00032, doi:10.3389/fped.2017.00032. This article has 35 citations.
(tian2022podocyteendocytosisin pages 1-2): Xuefei Tian, Patricia Bunda, and Shuta Ishibe. Podocyte endocytosis in regulating the glomerular filtration barrier. Frontiers in Medicine, Feb 2022. URL: https://doi.org/10.3389/fmed.2022.801837, doi:10.3389/fmed.2022.801837. This article has 32 citations.
(blaine2020regulationofthe pages 1-3): Judith Blaine and James Dylewski. Regulation of the actin cytoskeleton in podocytes. Cells, 9:1700, Jul 2020. URL: https://doi.org/10.3390/cells9071700, doi:10.3390/cells9071700. This article has 180 citations.
(agarwal2021renalcellmarkers pages 1-2): Shivangi Agarwal, Yashwanth R. Sudhini, Onur K. Polat, Jochen Reiser, and Mehmet M. Altintas. Renal cell markers: lighthouses for managing renal diseases. Dec 2021. URL: https://doi.org/10.1152/ajprenal.00182.2021, doi:10.1152/ajprenal.00182.2021. This article has 25 citations and is from a peer-reviewed journal.
(yu2018proteinurickidneydiseases pages 1-2): Samuel Mon-Wei Yu, Pitchaphon Nissaisorakarn, Irma Husain, and Belinda Jim. Proteinuric kidney diseases: a podocyte's slit diaphragm and cytoskeleton approach. Frontiers in Medicine, Sep 2018. URL: https://doi.org/10.3389/fmed.2018.00221, doi:10.3389/fmed.2018.00221. This article has 98 citations.
(preston2020arolefor pages 1-2): Rebecca Preston, Richard W Naylor, Graham Stewart, Agnieszka Bierzynska, Moin A Saleem, Martin Lowe, and Rachel Lennon. A role for ocrl in glomerular function and disease. Pediatric Nephrology (Berlin, Germany), 35:641-648, Dec 2020. URL: https://doi.org/10.1007/s00467-019-04317-4, doi:10.1007/s00467-019-04317-4. This article has 34 citations.