Overview of MAP7D1 (MAP7 Domain-Containing Protein 1)

MAP7D1 (MAP7 domain-containing protein 1) is a human microtubule-associated protein belonging to the MAP7 family of microtubule regulators (pmc.ncbi.nlm.nih.gov). This protein is also known by synonyms KIAA1187, RPRC1 (arginine/proline-rich coiled-coil protein 1), and PARCC1. It shares homology with MAP7 (also called ensconsin or E-MAP-115) and other paralogs MAP7D2 and MAP7D3, which together constitute the MAP7 family in mammals (pmc.ncbi.nlm.nih.gov). All MAP7 family members have a characteristic domain organization: two conserved coiled-coil domains separated by a proline/arginine-rich flexible linker (pmc.ncbi.nlm.nih.gov). The N-terminal domain (sometimes called the “MAP7 domain”) strongly binds microtubules, while the C-terminal domain can interact with the stalk region of kinesin motor proteins (pmc.ncbi.nlm.nih.gov). This bifunctional structure enables MAP7D1 to act as a scaffold on microtubules, linking them to motor proteins and other factors. MAP7D1 is a cytoplasmic protein predominantly localized to the cytoskeletal network, observed along microtubule filaments and enriched near microtubule organizing centers such as the centrosome (pmc.ncbi.nlm.nih.gov). By sequence and localization, it is closely related to the well-studied Drosophila ensconsin, reflecting an evolutionarily conserved role in microtubule regulation (pmc.ncbi.nlm.nih.gov).

Subcellular Localization: Consistent with its microtubule-binding role, MAP7D1 is found on cytoskeletal structures. It localizes to interphase microtubule networks and becomes concentrated on the mitotic spindle and midbody during cell division (as shown by similarity to other MAP7 proteins) . In cultured cells, MAP7D1 and its family members decorate microtubules with a gradient: highest at the centrosome/MT minus-end region and tapering off toward microtubule plus-ends (pmc.ncbi.nlm.nih.gov). This pattern suggests MAP7D1 may preferentially bind or stabilize the more proximal regions of microtubule bundles. MAP7D1 is also reported at the centrosome itself (pmc.ncbi.nlm.nih.gov), and its presence at the midbody during cytokinesis (the bridge of microtubules in dividing cells) has been inferred from homology . These localizations underscore that MAP7D1 operates in the cytoplasm, on microtubule structures, rather than in the nucleus or other organelles.

Microtubule Binding and Stabilization

Microtubule Stabilizing Protein: MAP7D1 functions as a microtubule-stabilizing protein that can modulate the dynamics of the microtubule cytoskeleton. Recent studies have demonstrated that MAP7D1 helps maintain a subset of stable, post-translationally modified microtubules in cells (www.genecards.org) (pmc.ncbi.nlm.nih.gov). In particular, MAP7D1 is required for the maintenance of acetylated microtubules, a hallmark of long-lived, stable microtubule fibers (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Knocking down MAP7D1 causes a reduction in overall levels of acetylated α-tubulin, without significantly affecting other microtubule modifications such as detyrosination (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Moreover, loss of MAP7D1 leads to a marked decrease in the intensity of acetylated tubulin around the centrosome, indicating that the integrity of stable microtubule arrays emanating from the centrosome depends on MAP7D1 (pmc.ncbi.nlm.nih.gov). In contrast, its close paralog MAP7D2 binds and stabilizes microtubules through a more direct mechanism and does not influence microtubule acetylation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These findings suggest that MAP7D1 promotes microtubule stability at least in part by supporting the acetylation and longevity of microtubule filaments, which in turn impacts cell structure and polarity.

Effects on Microtubule Dynamics: By stabilizing microtubules, MAP7D1 can modulate cell motility and morphology. In neuronal and fibroblast-like cell models, depletion of MAP7D1 was shown to disturb the balance of microtubule dynamics, leading to more labile microtubules and altered cell behavior (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Knockdown of MAP7D1 (or its paralog) increases the cell’s sensitivity to microtubule-depolymerizing agents like nocodazole, causing microtubule arrays to collapse more readily under stress (pmc.ncbi.nlm.nih.gov). Functionally, cells lacking MAP7D1 exhibit increased random cell migration and faster neurite outgrowth in neuronal cell studies (pmc.ncbi.nlm.nih.gov). This counterintuitive increase in motility upon losing a stabilizer is explained by the idea that highly dynamic (less stabilized) microtubules allow more exploratory growth of cell processes, albeit in a less directed manner (pmc.ncbi.nlm.nih.gov). Normally, MAP7D1’s stabilizing influence contributes to the formation of oriented, long-lived microtubules that foster directed cell movement and structured neurite extension, rather than random protrusions (pmc.ncbi.nlm.nih.gov). In summary, MAP7D1 helps maintain a stable microtubule scaffold, which is important for cell shape maintenance, polarity, and controlled migration.

Kinesin-1 Recruitment and Organelle Transport

One of the defining roles of the MAP7 family is regulation of the motor protein kinesin-1, and MAP7D1 is no exception. Kinesin-1 (conventionally KIF5 in mammals) is a major plus-end directed motor that ferries organelles and vesicles along microtubules. MAP7D1 and other MAP7 proteins act as microtubule-tethered kinesin activators, helping kinesin-1 engage with microtubule tracks (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In fact, all four mammalian MAP7 family members (MAP7, MAP7D1, MAP7D2, MAP7D3) have been shown to bind directly to kinesin-1 (pmc.ncbi.nlm.nih.gov). The C-terminal coiled-coil domain of MAP7D1 can attach to the stalk region of kinesin-1, while the MAP7D1 N-terminus simultaneously binds the microtubule, effectively bridging the motor to the microtubule (pmc.ncbi.nlm.nih.gov). This interaction greatly enhances the recruitment and processivity of kinesin-1. Experiments in cells demonstrate that without MAP7 proteins, kinesin-1 motors have difficulty attaching to microtubules and carrying cargo outward. For example, triple depletion of MAP7, MAP7D1, and MAP7D3 in HeLa cells caused a striking perinuclear clustering of mitochondria, phenocopying the loss of kinesin-1 function (pmc.ncbi.nlm.nih.gov). This indicates that these MAP7-family proteins are required for kinesin-driven organelle dispersion; in their absence, kinesin-1 cannot effectively transport cargo, leaving organelles stuck near the nucleus (pmc.ncbi.nlm.nih.gov). Notably, cells could not tolerate complete removal of all MAP7 paralogs – attempts to create a triple-knockout cell line of MAP7/MAP7D1/MAP7D3 were unsuccessful due to loss of viability (pmc.ncbi.nlm.nih.gov). This suggests that MAP7 family proteins perform essential cellular functions, likely by enabling vital kinesin-dependent transport processes.

Biochemical assays reinforce this model. In vitro reconstitution studies have shown that MAP7 proteins increase the frequency with which kinesin-1 motors land on microtubules and how far they travel. Purified MAP7D1 was not tested in detail in early studies, but MAP7 and MAP7D3 (which share the same domain architecture) dramatically enhanced kinesin’s ability to bind microtubules and move processively (pmc.ncbi.nlm.nih.gov). The mechanism appears to involve both direct tethering and allosteric activation. By transiently attaching to kinesin-1, MAP7D1 can keep the motor in proximity to the microtubule (facilitating frequent reattachment) and may induce a conformational change that relieves kinesin’s autoinhibition (pmc.ncbi.nlm.nih.gov). Hooikaas et al. (2019) proposed that MAP7 family members serve as “microtubule-tethered kinesin-1 activators”, meaning the motor briefly docks at MAP7 sites on the microtubule as it steps along (pmc.ncbi.nlm.nih.gov). This interaction is dynamic – for example, MAP7D3 was observed to even co-migrate with kinesin in some cases, due to its particularly high affinity for the motor (pmc.ncbi.nlm.nih.gov). Altogether, MAP7D1’s ability to bind both microtubules and kinesin positions it as a critical adaptor that promotes efficient cargo transport. This role is especially important in highly polarized or long cells (such as neurons or muscle cells) where kinesin-1 is needed for distributing organelles and molecules to the cell periphery (pmc.ncbi.nlm.nih.gov). Indeed, disruption of MAP7 family function in mouse muscle fibers led to mispositioned nuclei, underscoring the requirement of MAP7-mediated kinesin recruitment for proper intracellular transport (pmc.ncbi.nlm.nih.gov).

Roles in Cell Polarity, Signaling, and Cycle Control

Beyond its direct structural functions in the cytoskeleton, MAP7D1 has been implicated in several cellular signaling pathways and regulatory processes:

Wnt5a–DVL Signaling and Microtubule Remodeling: MAP7D1 participates in a feedback loop with the Wnt signaling pathway, particularly the non-canonical Wnt5a pathway. A 2018 study (Kikuchi et al., EMBO Reports) discovered that MAP7D1 (together with MAP7) interacts with Dishevelled (DVL), a key scaffold protein in Wnt signaling (pmc.ncbi.nlm.nih.gov). MAP7/MAP7D1 binding to DVL was found to facilitate microtubule remodeling in response to Wnt5a signals, and conversely, active Wnt5a signaling feeds back to influence microtubule organization via MAP7 proteins (pmc.ncbi.nlm.nih.gov). In essence, MAP7D1 and DVL form a positive feedback loop: Wnt5a signaling prompts changes in the microtubule cytoskeleton (possibly to aid cell polarity or migration), and MAP7D1 is a mediator of those cytoskeletal changes. Reciprocally, the state of the microtubule network (modulated by MAP7D1) can enhance or modulate the Wnt5a signal output. This cross-talk places MAP7D1 at the nexus of cytoskeletal dynamics and cell signaling, particularly in processes like planar cell polarity and cell movement that are driven by Wnt5a/DVL pathways.

NF-κB and Other Signaling in Cancer Cells: Emerging evidence links MAP7 family proteins to pro-migratory and pro-survival signaling in cancer contexts. In cervical carcinoma cells, MAP7 (Ensconsin) was shown to interact with RC3H1 (Roquin), an RNA-binding protein, and co-activate the NF-κB pathway, driving cancer cell proliferation and cell-cycle progression (pmc.ncbi.nlm.nih.gov). Another study in human cervical cancer reported that overexpression of MAP7 enhanced cell migration and invasion, potentially by modulating autophagy pathways that influence cell vitality and motility (pmc.ncbi.nlm.nih.gov). While these particular studies focused on MAP7 itself, MAP7D1 is highly similar and is co-expressed in many cell types (HeLa cervical cancer cells endogenously express MAP7D1 alongside MAP7) (pmc.ncbi.nlm.nih.gov). It is therefore plausible that MAP7D1 contributes to similar signaling outcomes. For instance, if MAP7D1 levels rise, it could reinforce cytoskeletal stability and vesicular transport in ways that favor cancer cell migration or NF-κB activation. Consistent with this idea, MAP7D1 has been found to act downstream of microRNAs and epigenetic regulators linked to cancer metastasis (discussed below). Overall, MAP7D1 may parallel MAP7 in supporting oncogenic signaling networks (like NF-κB) and cell motility mechanisms, although direct evidence for MAP7D1 in these specific pathways is still being uncovered.

Cell Cycle and DNA Damage Response: A surprising new function for MAP7D1 was recently identified in the context of the DNA damage response (DDR). Traditionally, DNA repair processes were thought to be confined to the nucleus, but an iScience 2023 study revealed that cytoskeletal proteins like MAP7D1 can influence DNA repair efficiency (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Using quantitative proteomics, Dullovi et al. (2023) found that MAP7D1 (and MAP7) interacts with several DNA double-strand break (DSB) repair proteins, including BRCA1, RAD50, 53BP1, MLH1, and XPC (pmc.ncbi.nlm.nih.gov). Notably, MAP7D1 was pulled down by phosphorylated peptides from BRCA1 in a kinase-specific manner, indicating a direct or indirect binding to activated DNA repair complexes (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Functionally, depleting MAP7D1 in G₁-phase cells led to a strong G₁ cell cycle arrest and impaired the repair of radiation-induced DSBs (pmc.ncbi.nlm.nih.gov). Cells lacking MAP7D1 showed reduced recruitment of RAD50 to damaged chromatin and fewer 53BP1 foci at DNA break sites, signifying a compromised DSB repair response (pmc.ncbi.nlm.nih.gov). These defects mirror those seen when microtubules are disrupted, suggesting that MAP7D1 provides a cytoplasmic support to nuclear DNA repair – perhaps by positioning repair factors or broken DNA segments via the LINC (cytoskeleton-nucleus linkage) complex (pmc.ncbi.nlm.nih.gov). The MAP7D1 region required for binding BRCA1/RAD50 overlaps with its coiled-coil domain, hinting that MAP7D1 might serve as a scaffold that transiently anchors repair proteins to microtubules or transports them within the cell (pmc.ncbi.nlm.nih.gov). This discovery expands the functional repertoire of MAP7D1: in addition to managing microtubule dynamics, it plays a part in maintaining genomic stability. It underscores a broader principle that cytoskeletal elements can actively contribute to DNA repair pathways, possibly by moving repair complexes or holding repair sites in favorable positions (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Such cross-talk between the cytoskeleton and genome surveillance mechanisms is an exciting area of current research.

Clinical and Biomedical Relevance

Cancer Progression and Prognosis: Given its roles in cell division, motility, and signaling, MAP7D1 has drawn attention in cancer biology. Aberrant expression of MAP7 family proteins is associated with tumor aggressiveness. For example, high MAP7 (ensconsin) expression has been identified as a poor prognostic marker in multiple cancers, including acute myeloid leukemia, colon and cervical cancers, and metastatic endometrial cancer (pmc.ncbi.nlm.nih.gov). Similarly, MAP7D1 has been implicated in cancer proliferation and metastasis. A 2021 epigenomic study identified MAP7D1 as a novel regulator of lymph node metastasis in breast cancer (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In that study, primary breast tumors with lymph-node metastases showed significantly elevated 5-hydroxymethylcytosine (5hmC) marks at the MAP7D1 gene and correspondingly higher MAP7D1 expression (academic.oup.com) (academic.oup.com). The 5hmC enrichment at MAP7D1 correlated positively with the metastatic capability of tumors, and follow-up experiments demonstrated that altering MAP7D1 levels could affect breast cancer cell invasiveness (academic.oup.com) (academic.oup.com). In practical terms, overexpression of MAP7D1 promotes breast cancer cell proliferation and migration, whereas silencing MAP7D1 tends to impair these malignant traits (pmc.ncbi.nlm.nih.gov). These findings suggest that MAP7D1 helps tumor cells maintain the robust cytoskeletal dynamics and transport functions needed for metastasis. It may facilitate the extreme polarization and motility required for cancer cells to intravasate and colonize new sites. As such, MAP7D1 is being examined as a potential biomarker for metastatic propensity and even as a therapeutic target. If disrupting MAP7D1 can reduce metastasis (as initial cell studies indicate), then drugs that inhibit MAP7D1 interactions (for instance, blocking its binding to kinesin or tubulin) might have anti-metastatic effects.

Neurobiology and Other Contexts: MAP7D1 is also of interest in neurobiology, since microtubule stability and cargo transport are critical in neurons. MAP7D1 (and MAP7D2) are expressed in the brain, with MAP7D1 detected in both developing neurites and mature neuronal cells (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The distinct ways that MAP7D1 stabilizes microtubules (via acetylation) vs. MAP7D2 (via direct binding) may reflect specialized roles in neurons — for instance, MAP7D1 might regulate long-term stability of select microtubule tracks (important for maintaining axon structure or synaptic delivery), whereas MAP7D2 might govern rapid dynamic remodeling. Indeed, the balance of these proteins can affect neurite outgrowth: removing MAP7D1 caused neurons to extend processes more rapidly but in a less directed fashion (pmc.ncbi.nlm.nih.gov). This could have implications for neural development or regeneration. Although not yet linked to specific neurological disorders, any disruption in microtubule transport (to which MAP7D1 contributes) could play a role in neurodegenerative disease mechanisms (by analogy to transport defects seen in ALS, Alzheimer’s, etc.). Research is ongoing to map out where MAP7D1 is expressed in the brain and its potential interactions with neuronal cargoes or motors.

Expert Perspectives: Scientists in the field underscore the significance of MAP7D1 as a versatile cytoskeletal effector. In a 2019 Journal of Cell Biology article, Akhmanova and colleagues described MAP7 proteins as crucial positive regulators of kinesin-based transport, contrasting them with classical MAPs like tau that inhibit motors (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). They proposed that the ensconsin/MAP7 family provides a “transport-friendly” microtubule surface that enables efficient long-range trafficking in cells (pmc.ncbi.nlm.nih.gov). More recent expert analyses (2023) highlight the expanding scope of MAP7D1’s functions, noting it as one of the “cytoskeleton-related proteins involved in DNA repair”, a concept that broadens our understanding of genome maintenance (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The convergence of roles – from microtubule stabilization and motor recruitment to signaling and DNA repair – makes MAP7D1 an interesting example of a multitasking cellular protein. As one study summarized, “Taken together, these findings describe for the first time an important function of MAP7 and MAP7D1 in cell cycle regulation and the cellular response to DNA damage” (pmc.ncbi.nlm.nih.gov). This multifaceted profile means MAP7D1 is now studied by cell biologists, cancer researchers, and others from different angles.

Recent Advances and Future Directions

Research on MAP7D1 has accelerated in the last few years, bringing new insights into its function:

• 2022–2023 Discoveries: The role of MAP7D1 in microtubule stabilization was firmly demonstrated in 2022 by showing its specific requirement for sustaining acetylated microtubules and restraining random cell motility (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In early 2023, the unanticipated involvement of MAP7D1 in DNA double-strand break repair was reported, suggesting a novel cytoskeleton-genome interaction mechanism (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These cutting-edge findings (published in Life Science Alliance, 2022 and iScience, 2023) have expanded the functional annotation of MAP7D1 beyond the traditional view of a microtubule motor adaptor.

• Ongoing Research: Scientists are now probing how MAP7D1 mechanistically influences these processes. Structural biology approaches are being applied to understand how the MAP7 domain binds tubulin. A 2024 structural study on the core MAP7 microtubule-binding domain revealed how it docks along the microtubule lattice and engages tubulin tails at an atomic level (www.nature.com) (www.nature.com). Although that work focused on MAP7, the conserved domains mean MAP7D1 likely binds microtubules in a similar fashion. Further, given differences between family members, ongoing research aims to map which regions of MAP7D1 bind kinesin-1 versus other partners (like BRCA1 or DVL). The goal is to pinpoint interaction interfaces that could be targeted by inhibitors. For example, interfering with the MAP7D1–kinesin interaction might selectively attenuate tumor cell motility. Early druggability studies are looking at small molecules that disrupt MAP7 interactions with motors or tubulin, though this is still in preliminary stages.

• Functional Genomics and Disease Links: High-throughput screens and genomics are also shedding light on MAP7D1. CRISPR knockout phenotypes in cell lines hint at roles in viral infection susceptibility and pancreatic cell viability (www.genecards.org), though these findings need validation. In cancer genomics, MAP7D1 gene alterations are not common drivers, but changes in its expression (epigenetic or transcriptional) can influence disease outcome (academic.oup.com) (academic.oup.com). As researchers profile more tumors, MAP7D1 could emerge as part of a signature for metastatic potential. There is also interest in whether MAP7D1 polymorphisms or expression differences contribute to variability in neuron regeneration or in disorders of cell migration (like developmental anomalies).

In summary, MAP7D1 is a multifunctional cytoskeletal protein that stabilizes microtubules, activates motor-based transport, and even interfaces with cell signaling and DNA repair pathways. Its activity is central to maintaining cellular infrastructure and responding to stress. Ongoing studies, especially those in the past two years, have significantly advanced our understanding of MAP7D1. This protein exemplifies how cells repurpose structural components for regulatory roles – a concept with broad implications for cell biology and medicine. As research continues, MAP7D1 may become a target of therapeutic interest (for example, in metastatic cancer) and a factor to consider in diseases rooted in cytoskeletal dysfunction. The current trajectory of MAP7D1 research is poised to deliver deeper mechanistic insights and potentially novel strategies for intervention, making it a prime candidate for functional annotation updates in genomic databases in light of the latest scientific evidence.

References: (Publication dates and sources are included in citations)

Citations

1. AnnotationURLCitation(end_index=344, start_index=200, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=Monroy%20et%20al,Additional%20regions%20with%20MT%20affinity')
2. AnnotationURLCitation(end_index=785, start_index=641, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=Monroy%20et%20al,Additional%20regions%20with%20MT%20affinity')
3. AnnotationURLCitation(end_index=1104, start_index=941, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=MAP7D1%2C%20MAP7D2%2C%20and%20MAP7D3,flies%2C%20ensconsin%20is%20an%20essential')
4. AnnotationURLCitation(end_index=1437, start_index=1291, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=have%20a%20similar%20organization%2C%20with,2008%20%3B%20%2034')
5. AnnotationURLCitation(end_index=1894, start_index=1768, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=its%20subcellular%20localization,regulated')
6. AnnotationURLCitation(end_index=2163, start_index=2060, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=Monroy%20et%20al,It')
7. AnnotationURLCitation(end_index=2779, start_index=2653, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=its%20subcellular%20localization,regulated')
8. AnnotationURLCitation(end_index=3119, start_index=2950, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=Map7D2%20stabilizes%20MTs%20to%20control,balance%20between%20MT%20stabilization%20and')
9. AnnotationURLCitation(end_index=3862, start_index=3735, title='MAP7D1 Gene - GeneCards | MA7D1 Protein | MA7D1 Antibody', type='url_citation', url='https://www.genecards.org/cgi-bin/carddisp.pl?gene=MAP7D1#:~:text=%2A%20Microtubule,MA7D1_HUMAN%2CQ3KQU3')
10. AnnotationURLCitation(end_index=4028, start_index=3863, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=the%20effects%20of%20Map7d2%20or,acetylated%20but%20not%20detyrosinated%20tubulin')
11. AnnotationURLCitation(end_index=4335, start_index=4168, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=Map7D2%2C%20Map7D1%20is%20required%20to,cell%20motility%20and%20neurite%20outgrowth')
12. AnnotationURLCitation(end_index=4517, start_index=4336, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=knockdown%20greatly%20decreased%20the%20intensity,the%20maintenance%20of%20acetylated%2C%20stable')
13. AnnotationURLCitation(end_index=4854, start_index=4689, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=the%20effects%20of%20Map7d2%20or,acetylated%20but%20not%20detyrosinated%20tubulin')
14. AnnotationURLCitation(end_index=5009, start_index=4855, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=We%20also%20found%20that%20among,2003%3B%20Sudo%20%26%20Baas%2C%202010')
15. AnnotationURLCitation(end_index=5403, start_index=5232, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=match%20at%20L496%20knockdown%20greatly,the%20maintenance%20of%20acetylated%2C%20stable')
16. AnnotationURLCitation(end_index=5754, start_index=5556, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=agent%20nocodazole%20without%20affecting%20acetylated%2Fdetyrosinated,balance%20between%20MT%20stabilization%20and')
17. AnnotationURLCitation(end_index=5922, start_index=5755, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=Map7D2%2C%20Map7D1%20is%20required%20to,cell%20motility%20and%20neurite%20outgrowth')
18. AnnotationURLCitation(end_index=6592, start_index=6434, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=Map7D2%20and%20Map7D1,facilitate%20MT%20stabilization%20through%20distinct')
19. AnnotationURLCitation(end_index=6747, start_index=6593, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=We%20also%20found%20that%20among,2003%3B%20Sudo%20%26%20Baas%2C%202010')
20. AnnotationURLCitation(end_index=7110, start_index=6942, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=Map7D2%20localized%20prominently%20to%20the,contrast%20to%20Map7D2%2C%20Map7D1%20was')
21. AnnotationURLCitation(end_index=7403, start_index=7245, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=Map7D2%20and%20Map7D1,facilitate%20MT%20stabilization%20through%20distinct')
22. AnnotationURLCitation(end_index=7785, start_index=7631, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=We%20also%20found%20that%20among,2003%3B%20Sudo%20%26%20Baas%2C%202010')
23. AnnotationURLCitation(end_index=8152, start_index=7998, title='Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9039348/#:~:text=We%20also%20found%20that%20among,2003%3B%20Sudo%20%26%20Baas%2C%202010')
24. AnnotationURLCitation(end_index=8873, start_index=8744, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=found%20that%20all%20four%20mammalian,binding')
25. AnnotationURLCitation(end_index=8998, start_index=8874, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=N,as%20it%20moves%20along%20microtubules')
26. AnnotationURLCitation(end_index=9223, start_index=9127, title='MAP7 family proteins regulate kinesin-1 recruitment and activation - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC6446838/#:~:text=Kinesin,MAP7')
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