RAB9A (Ras-related protein Rab-9A) – Function and Role in Human Cells OpenAI o3-deep-research-2025-06-26 113 citations 2025-12-27T21:13:15.903307

RAB9A (Ras-related protein Rab-9A) – Function and Role in Human Cells

Key Concepts and Definitions

RAB9A is a human gene encoding Rab9A, a small GTP-binding protein of the Rab family within the Ras superfamily. Rab proteins act as molecular switches that cycle between an inactive GDP-bound state and an active GTP-bound state, recruiting specific effector proteins to membranes when GTP-bound (go.drugbank.com). Like other Rab GTPases, Rab9A contains a P-loop NTP-binding domain (Ras domain) and is post-translationally prenylated at its C-terminus (dual cysteine motif), anchoring it to cellular membranes (go.drugbank.com). Rab9A is one of over 60 Rab proteins in humans (pmc.ncbi.nlm.nih.gov), each directing vesicle trafficking steps in distinct intracellular pathways.

Rab9A is best known for its role in retrograde transport – specifically, the recycling of mannose-6-phosphate receptors (MPRs) from late endosomes back to the trans-Golgi network (TGN) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This process is critical for lysosomal enzyme sorting: MPRs capture acid hydrolases in the Golgi and release them in endosomes; Rab9A then helps return the empty MPRs to the TGN for reuse (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Consistent with this role, Rab9A localizes chiefly to late endosomal membranes (with inactive pools in the cytosol). It is part of the small GTPase Rab family, sharing ~87% sequence identity with its paralog Rab9B (pmc.ncbi.nlm.nih.gov). (Rab9A is sometimes simply called “Rab9”; in humans “Rab9” generally refers to Rab9A (pmc.ncbi.nlm.nih.gov).) Rab9A is classified under enzyme code EC 3.6.5.2 as a GTP phosphohydrolase, though its cellular function is regulatory – toggling between GTP and GDP to control membrane trafficking rather than catalyzing metabolic reactions (pubmed.ncbi.nlm.nih.gov).

Mechanistically, Rab9A-GTP assembles dedicated machinery on the cytosolic face of late endosomes. It directly binds effector proteins that mediate vesicle movement and tethering. Key effectors include TIP47 (tail-interacting protein of 47 kDa), which Rab9A recruits to endosomal membranes to capture cargo receptors, and the GCC185 golgin tether on the TGN, which helps dock Rab9-positive vesicles at the Golgi (pmc.ncbi.nlm.nih.gov). Through these interactions, Rab9A facilitates the efficient delivery of cargo like cation-independent MPR (CI-MPR) from endosomes to the TGN. In line with this, blocking Rab9A function (e.g. using dominant-negative mutants or knockdown) causes CI-MPR to accumulate in endosomes and impairs lysosomal enzyme recycling (pmc.ncbi.nlm.nih.gov). Additionally, Rab9A’s activity relies on regulatory proteins: it is activated by a specific guanine-nucleotide exchange factor (GEF) – the DENND2 family – which loads Rab9 with GTP on endosomal membranes (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov), and likely inactivated by one or more Rab GTPase-activating proteins (GAPs) such as RUTBC1/2 (which are themselves Rab9A-binding proteins) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These layers of regulation ensure Rab9A is active at the right place and time to govern vesicle trafficking.

Biological Function and Localization

Rab9A’s primary biological function is to regulate endosome-to-Golgi transport. It is enriched on late endosomes, a compartment in which it segregates into specific subdomains distinct from those of Rab7 (the major late endosome/lysosome Rab) (pmc.ncbi.nlm.nih.gov). Rab9A is not required for the general maturation of endosomes into lysosomes – that role belongs to Rab7 – but instead Rab9A ensures select cargo are retrieved from late endosomes before degradation (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In particular, Rab9A is crucial for sorting lysosomal enzymes: it helps return mannose-6-phosphate receptors and other recycling proteins from late endosomes to the TGN, thereby indirectly affecting the delivery of enzymes to lysosomes (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Cells lacking Rab9A function show mis-sorting of these receptors and can have defects in lysosome function and morphology (pmc.ncbi.nlm.nih.gov). Experiments have demonstrated that adding active Rab9A (or its effectors) can stimulate in vitro vesicle transport from endosomes to Golgi (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov), underscoring its role as a rate-limiting factor in this pathway.

Rab9A is anchored to the cytosolic face of membranes via geranylgeranyl lipids on its C-terminus. In the GDP-bound form, Rab9A is extracted from membranes by GDP-dissociation inhibitor (GDI) and held soluble in the cytosol (pmc.ncbi.nlm.nih.gov). Upon activation (GDP–>GTP exchange) by its GEF on late endosomes, Rab9A inserts into the late endosomal membrane and organizes trafficking complexes. Approximately 20–30% of Rab9A (and its effector p40/TIP47) can be found on membranes at any time, with the remainder in cytosolic pools that exchange with the membrane-bound fraction (pmc.ncbi.nlm.nih.gov). Rab9A-positive late endosomes often travel along microtubules toward the cell center (Golgi region). Indeed, active Rab9A links these organelles to the dynein motor: recent studies showed that Nde1/Ndel1, a dynein adapter protein, serves as a Rab9A effector that tethers late endosomes to dynein/dynactin complexes for movement toward the TGN (pubmed.ncbi.nlm.nih.gov). Crystal structures of Rab9A in complex with Nde1 reveal the molecular interface by which GTP-bound Rab9A recruits the Nde1-Lis1-dynein assembly (pubmed.ncbi.nlm.nih.gov). Without Rab9A or Nde1, late endosomes fail to engage dynein and cannot efficiently move to or fuse with the Golgi (pubmed.ncbi.nlm.nih.gov).

Beyond the conventional endosome-TGN route, Rab9A also participates in specialized trafficking pathways. In pigment cells (melanocytes), Rab9A localizes to melanosomes (lysosome-related organelles for melanin storage) and is required for delivering enzymes like tyrosinase (TYR), TYRP1, and DCT to these melanosomes (go.drugbank.com). Rab9A knockdown in melanocytes causes hypopigmentation, as melanosomal proteins are misrouted to lysosomes instead of being incorporated into melanosomes (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Notably, Rab9A’s role in melanocytes works in concert with other melanosomal Rabs (Rab38/Rab32) and their effectors. Rab9A depletion phenocopies the loss of Rab38/32 or the BLOC-3 complex – all resulting in shortened endosomal tubules and cargo mis-targeting – suggesting Rab9A acts alongside those factors to generate the tubules that ferry cargo to maturing melanosomes (pmc.ncbi.nlm.nih.gov). This underscores a broader role for Rab9A in lysosome-related organelle biogenesis, ensuring that cargo is sorted correctly for organelles like melanosomes and perhaps secretory granules (pmc.ncbi.nlm.nih.gov).

Rab9A has also been implicated in forms of autophagy. Specifically, an alternative macroautophagy pathway (often called Atg5/Atg7-independent autophagy) relies on Rab9. In this non-canonical pathway, Rab9A-positive membranes from the TGN or late endosomes help form autophagosome-like vesicles without using the LC3 conjugation system (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). For instance, under certain stress conditions cells can generate autophagosomes by a Rab9-dependent fusion of isolation membranes with late endosomal/TGN membranes (pmc.ncbi.nlm.nih.gov). Recent research has identified TMEM9, a lysosomal protein, as an upstream regulator that activates Rab9-dependent autophagosome formation: TMEM9 interacts with the Beclin1 complex and, by freeing Beclin1 from its inhibitor Bcl-2, triggers Rab9A-dependent, LC3-independent autophagy (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). In cells overexpressing TMEM9, Rab9A and the Beclin1 complex co-localize on late endosomal/lysosomal compartments, leading to increased formation of these alternative autophagosomes (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). Thus, Rab9A plays a role in a backup autophagic route, linking late endosomal membranes to the autophagy machinery in times of stress or when canonical autophagy is compromised.

Recent Developments (2023–2024)

Continued research in 2023–2024 has expanded our understanding of Rab9A’s functions and its involvement in disease-relevant processes. One notable 2023 study uncovered a noncanonical role of Rab9A in viral infection. Researchers investigating human papillomavirus (HPV) entry found that, unlike its supportive role for cellular cargo, Rab9A in its active GTP-bound form actually hinders HPV trafficking (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In HPV-infected cells, GTP-bound Rab9A appears to delay the virus’s escape from endosomes by modulating the virus’s interaction with the retromer complex (pmc.ncbi.nlm.nih.gov). When Rab9A was knocked down, HPV showed increased binding to retromer and improved transport from endosomes to the Golgi, ultimately enhancing infection (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Paradoxically, an excess of active Rab9A (GTP-locked mutant) was found to impair HPV entry, while an excess GDP-locked Rab9A mutant stimulated HPV’s transfer to the Golgi (pmc.ncbi.nlm.nih.gov). These findings suggest HPV subverts the host trafficking pathway in a unique way – it benefits from Rab9A being turned off at a certain step, unlike cellular MPR transport which requires Rab9A on. This 2023 discovery highlights the sophisticated interplay between viruses and Rab9A-dependent pathways, and it suggests that Rab9A’s activity must be precisely tuned during viral entry.

Another line of recent research has focused on Rab9A’s role in autophagy and organelle dynamics. A 2022 structural biology study provided high-resolution insight into how Rab9A connects to the dynein motor: by solving the crystal structure of GTP-bound Rab9A bound to an Nde1 peptide, researchers confirmed that Nde1 directly recognizes Rab9A’s switch regions (pubmed.ncbi.nlm.nih.gov). They pinpointed key Rab9A residues required for Nde1 binding, and showed that mutating those residues prevents Rab9A from recruiting the dynein–Lis1 complex (pubmed.ncbi.nlm.nih.gov). Functionally, cells expressing Rab9A mutants defective in Nde1-binding failed to transport late endosomes to the perinuclear TGN area (pubmed.ncbi.nlm.nih.gov). This 2022 work (published in early 2022, with an e-print in 2021) solidified Nde1/Ndel1 as bona fide effectors of Rab9A that bridge vesicles to motor proteins, filling a gap in our understanding of Rab9A’s role in retrograde traffic.

In the realm of autophagy, very recent findings (2023–2024) have linked Rab9A to mitophagy (selective autophagy of mitochondria) and cardioprotection. Building on the discovery of TMEM9’s activation of Rab9-dependent autophagy (pubmed.ncbi.nlm.nih.gov), studies in 2023 reported that an Ulk1-Rab9-Beclin1 signaling axis mediates alternative mitophagy in heart tissue (pmc.ncbi.nlm.nih.gov). This pathway can help remove damaged mitochondria during ischemic stress, suggesting Rab9A contributes to cell survival under metabolic stress. Such insights are quite new, and ongoing research aims to delineate how Rab9A cooperates with canonical autophagy proteins versus when it acts independently. The emerging theme is that Rab9A serves as a flexible trafficking hub that can be co-opted or regulated in various contexts – from virus infection to organelle quality control – beyond its classical housekeeping role in protein sorting.

Current Applications and Real-World Implications

While Rab9A itself is a fundamental cell biology factor (not a drug or technology), understanding its function has real-world implications in medicine and biotechnology. One important area is infectious disease: multiple pathogens hijack the Rab9A-dependent pathway for their own replication. For example, research has shown that Rab9A is required for the life cycles of HIV-1, Ebola and Marburg filoviruses, and measles virus (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In a cell-based study, disabling Rab9 (via gene trap mutation or siRNA) allowed cells to survive otherwise-lethal Marburg virus infection – implicating Rab9A-mediated trafficking as essential for viral assembly or egress (pmc.ncbi.nlm.nih.gov). Follow-up experiments revealed that Rab9A depletion severely reduces the production of HIV viral particles and other enveloped viruses. This suggests that Rab9A could be a potential broad-spectrum antiviral target: if a drug could transiently inhibit Rab9A function in infected cells, it might block viruses from assembling or exiting host organelles (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Indeed, silencing RAB9A in human cells led to an ~80–90% drop in HIV-1 particle release (as measured by HIV p24 antigen) and a ~70–75% reduction in infectious Ebola virus output, compared to control cells (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These striking effects underscore Rab9A’s importance for viruses that exploit the late endosome-TGN network. However, because Rab9A is also crucial for normal cell function, any antiviral strategy would need to carefully target the virus-Rab9 interaction (for instance, disrupting a viral protein’s ability to usurp Rab9A or its effector TIP47) to avoid toxic effects on host cells.

Rab9A has also drawn interest in the context of human disease and therapy, particularly cancer and neurodegeneration. In cancer biology, Rab9A’s role in trafficking and autophagy intersects with pathways that tumor cells often modulate. A recent study in hepatocellular carcinoma found that RAB9A expression is upregulated in some liver tumors and that Rab9A appears to promote oncogenic behavior in cancer cells (pmc.ncbi.nlm.nih.gov). For example, forced overexpression of Rab9A in liver cancer cell lines enhanced their proliferation, colony formation, and invasive migration, while Rab9A knockdown had the opposite effect, suppressing growth and inducing apoptosis (pmc.ncbi.nlm.nih.gov). Mechanistically, Rab9A overexpression was associated with activation of the AKT/mTOR signaling pathway in these cells (pmc.ncbi.nlm.nih.gov). Although the exact link between Rab9A’s trafficking function and AKT/mTOR signaling is still being explored, one hypothesis is that Rab9A might affect the turnover of growth factor receptors or the autophagy flux in a way that modulates pro-survival signals. This makes Rab9A a candidate biomarker for aggressive cancer behavior, and if further validated, components of the Rab9A pathway (like specific effectors or regulators) could be investigated as drug targets to impair tumor cell survival. It’s worth noting that Rab9A itself is a small intracellular protein and not easily “druggable,” but its critical position in trafficking networks means upstream or downstream nodes (such as the DENND2 GEF or interactions with motors) might be targeted by small molecules in the future to influence outcomes in diseases.

In neurodegenerative diseases, dysfunctions in endosomal trafficking are a common theme (e.g. Alzheimer’s disease and others show endosome anomalies). While Rab9A has not been as strongly linked to specific genetic neurodegenerative disorders as some other Rabs (Rab7 mutations cause Charcot–Marie–Tooth neuropathy, for instance (pmc.ncbi.nlm.nih.gov)), there is evidence that Rab9A may contribute to neuronal homeostasis. Its role in retrograde transport to the Golgi is relevant for neurons, which rely on long-range vesicle transport. Studies in cell models suggest that perturbing Rab9A function can lead to accumulation of proteins in late endosomes and possibly impact lysosome function (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Moreover, Rab9A’s involvement in alternative autophagy might intersect with the removal of protein aggregates or damaged organelles in neurons – processes crucial in preventing neurodegeneration. Thus, some researchers are examining Rab9A’s activity in models of diseases like Parkinson’s or certain forms of dementia where endolysosomal traffic and autophagy are impaired. Although this research is still in early stages, it reflects a broader real-world interest: modulating Rab9A pathways could potentially ameliorate diseases that involve trafficking defects.

From a biotechnological standpoint, Rab9A and its effectors have been used as tools to dissect membrane traffic. For instance, researchers use dominant-negative Rab9A mutants (Rab9 S21N, a GDP-locked form) to intentionally block endosome-to-TGN transport and then observe how this affects the distribution of proteins like MPRs or toxins – helping to map out the retrograde trafficking routes (pmc.ncbi.nlm.nih.gov). Rab9A-positive vesicles have also been analyzed in cell-free systems to reconstitute docking and fusion events with Golgi membranes (pmc.ncbi.nlm.nih.gov). These experimental systems provide platforms for testing inhibitors or investigating how altering traffic can change cell physiology. In summary, while you won’t find Rab9A in a clinical setting by itself, our growing knowledge of Rab9A’s network is informing multiple arenas – from antiviral strategies to cancer research – making this small GTPase a significant node connecting cell biology to real-world health outcomes.

Expert Opinions and Analysis from Authoritative Sources

Experts in the field of membrane trafficking have long recognized Rab9A as a paradigm for Rab GTPase function in endosomal transport. In a classic 2001 Science article, Pfeffer and colleagues demonstrated that Rab9 (Rab9A) increases the affinity of its effector TIP47 for the mannose-6-phosphate receptor, thereby markedly enhancing MPR recycling to the Golgi (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This discovery was among the first to show how a Rab protein can actively recruit a cargo adaptor to sort specific receptors. As Dr. Suzanne Pfeffer (a leading authority on Rab GTPases) noted, Rab9A essentially serves as a matchmaker between cargo and carrier: the GTP-bound Rab9A on endosomal membranes binds TIP47, which in turn captures the cytoplasmic tails of MPRs, assembling a transport complex that directs the vesicle to the TGN (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Such insights have cemented Rab9A’s reputation as a key regulator ensuring vital cargo is returned to the Golgi rather than lost to lysosomal degradation.

Recent authoritative reviews continue to emphasize Rab9A’s central role and elaborate on its network of interactions. A 2022 comprehensive review in Computational and Structural Biotechnology Journal summarized that “Rab9A, together with its effectors TIP47 and GCC185, is required to transport CI-MPRs from late endosomes to the TGN”, highlighting that without Rab9A, cells cannot efficiently recycle these receptors (pmc.ncbi.nlm.nih.gov). The same review also pointed out the intriguing cooperation between Rab9A and Rab7 on late endosomes: while they occupy distinct microdomains, they coordinate to balance recycling vs. degradation pathways (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The authors underscore that Rab9A is not simply redundant to Rab7 but has unique effectors and timing – for example, Rab9A’s presence on a late endosomal domain signals that a vesicle is destined for the Golgi, and it likely has to be inactivated (or displaced) once that vesicle fuses at the TGN in order to release its cargo (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This notion aligns with expert analyses that trafficking routes are tightly regulated by sequential Rab conversions (often called Rab cascades) where one Rab’s effectors can recruit the next Rab’s GEF or GAP (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In Rab9A’s case, there is evidence that its effectors like RUTBC1/2 double as GAPs for other Rabs (Rab32, Rab33, Rab36), suggesting Rab9A might facilitate the hand-off or termination of one pathway as cargo enters the next (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Disease-focused experts have also weighed in on Rab9A. In virology circles, Rab9A is often cited as a “host dependency factor” for viruses. Virologist Daniel DiMaio, in commenting on the 2023 HPV study, remarked that it was surprising to find Rab9A acting as a restriction factor when GTP-bound, since traditionally Rab9A was thought to always promote cargo transport (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This observation led experts to propose a model where HPV L2 capsid protein might stall on Rab9-coated domains to avoid premature endosome exit, essentially hacking the Rab9A system to time its delivery to the TGN for successful infection. Such nuanced perspectives illustrate that expert understanding of Rab9A is evolving – it is not merely a housekeeping protein, but a point of crosstalk that pathogens and specialized cell processes can manipulate.

Finally, thought leaders in cell biology like Harald Stenmark have framed Rab9A in the larger context of endosomal Rab circuits. In a Nature Reviews article, Stenmark and colleagues listed Rab9 alongside Rab7, Rab4, Rab11, etc., as core coordinators of endosomal traffic, each occupying a characteristic zone and function (pmc.ncbi.nlm.nih.gov). They note that Rab9 (A) helps define a route for retrieval to the Golgi, distinguishing it from Rab7’s route to degradation (pmc.ncbi.nlm.nih.gov). Rab9A’s presence on an organelle can thus be seen as a marker of “salvage” pathways in the cell. Authoritative sources agree that without Rab9A, cells lose efficiency in reclaiming important receptors and enzymes – a failure that can have ripple effects on cellular metabolism and signaling (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The consensus in expert analyses is clear: Rab9A is an essential organizer of late endosomal trafficking, whose activity must be precisely regulated. Its study not only illuminates basic cell biology but also provides insight into how cells maintain balance between recycling and degradation, how pathogens exploit cellular logistics, and how trafficking imbalances might contribute to disease.

Relevant Statistics and Data from Recent Studies

References: The information above is drawn from current scientific literature and databases, including peer-reviewed journal articles and authoritative reviews. Key sources include Journal of Cell Biology (Díaz et al., 1997) (pmc.ncbi.nlm.nih.gov), Science (Carroll et al., 2001) (pmc.ncbi.nlm.nih.gov), Molecular Biology of the Cell (Barrowman et al., 2006) (go.drugbank.com), Journal of Virology (Murray et al., 2005) (pmc.ncbi.nlm.nih.gov), Pigment Cell Melanoma Research (Mahanty et al., 2016) (pmc.ncbi.nlm.nih.gov), PLoS Pathogens (Choi & DiMaio, 2023) (pmc.ncbi.nlm.nih.gov), Nature Communications (Okada et al., 2023) (pubmed.ncbi.nlm.nih.gov), and comprehensive reviews in Nat. Rev. Mol. Cell Biol. and Comput. Struct. Biotechnol. J. (2022) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Publication dates range from foundational studies in the 1990s to the most recent findings in 2023, reflecting the evolving understanding of Rab9A’s function, regulation, and importance in cellular physiology and disease. Each citation above includes a link to the source and, where available, the publication year for reference.

Citations

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  21. AnnotationURLCitation(end_index=6615, start_index=6492, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=are%20required%20to%20transport%20CI,23')
  22. AnnotationURLCitation(end_index=6901, start_index=6739, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=is%20also%20known%20to%20play,retrograde%20trafficking%20of%20late%20endosomes')
  23. AnnotationURLCitation(end_index=7224, start_index=7042, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=identify%20proteins%20that%20interact%20preferentially,vitro%20transport%20assay%20that%20measures')
  24. AnnotationURLCitation(end_index=7382, start_index=7225, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=transport%20of%20mannose%206,process%20of%20transport%20vesicle%20docking')
  25. AnnotationURLCitation(end_index=7851, start_index=7673, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=identify%20proteins%20that%20interact%20preferentially,in%20that%20the%20pure%2C%20recombinant')
  26. AnnotationURLCitation(end_index=8363, start_index=8186, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=roughly%20fourfold%20preference%20to%20Rab9%E2%80%93GDP,confirmed%20by%20the%20finding%20that')
  27. AnnotationURLCitation(end_index=8877, start_index=8716, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=retrograde%20transport%20remains%20unclear,retrograde%20transport%20to%20the%20TGN')
  28. AnnotationURLCitation(end_index=9184, start_index=9023, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=retrograde%20transport%20remains%20unclear,retrograde%20transport%20to%20the%20TGN')
  29. AnnotationURLCitation(end_index=9457, start_index=9300, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=interact%20with%20the%20dynein%20motor,retrograde%20transport%20to%20the%20TGN')
  30. AnnotationURLCitation(end_index=9909, start_index=9780, title='Ras-related protein Rab-9A | DrugBank Online', type='url_citation', url='https://go.drugbank.com/polypeptides/P51151#:~:text=uses%20NDE1%2FNDEL1%20as%20an%20effector,By%20similarity')
  31. AnnotationURLCitation(end_index=10240, start_index=10069, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=regulate%20these%20trafficking%20steps%2C%20the,targeted%20the%20SNARE%20to%20lysosomes')
  32. AnnotationURLCitation(end_index=10377, start_index=10241, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=Rab9A,cargo%20delivery%20to%20maturing%20melanosomes')
  33. AnnotationURLCitation(end_index=10887, start_index=10751, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=knockdown%20in%20melanocytes%20results%20in,mediated')
  34. AnnotationURLCitation(end_index=11196, start_index=11080, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=share%2087%C2%A0,Golgi%20network')
  35. AnnotationURLCitation(end_index=11679, start_index=11540, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=In%20addition%2C%20Rab9,is%20unclear%20how%20Rab7%20and')
  36. AnnotationURLCitation(end_index=11851, start_index=11680, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=Rab9%20are%20differentiated%20and%20recovered%2C,to%20the%20development%20of%20multiple')
  37. AnnotationURLCitation(end_index=12169, start_index=12017, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=match%20at%20L339%20In%20addition%2C,is%20unclear%20how%20Rab7%20and')
  38. AnnotationURLCitation(end_index=12591, start_index=12457, title='TMEM9 activates Rab9-dependent alternative autophagy through interaction with Beclin1 - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/39078420/#:~:text=identified,that%20multiple%20glycosylation%20of%20TMEM9')
  39. AnnotationURLCitation(end_index=12715, start_index=12592, title='TMEM9 activates Rab9-dependent alternative autophagy through interaction with Beclin1 - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/39078420/#:~:text=autophagy,the%20Beclin1%20complex%20at%20the')
  40. AnnotationURLCitation(end_index=13033, start_index=12899, title='TMEM9 activates Rab9-dependent alternative autophagy through interaction with Beclin1 - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/39078420/#:~:text=identified,that%20multiple%20glycosylation%20of%20TMEM9')
  41. AnnotationURLCitation(end_index=13176, start_index=13034, title='TMEM9 activates Rab9-dependent alternative autophagy through interaction with Beclin1 - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/39078420/#:~:text=autophagy,autophagosome%20to%20induce%20alternative%20autophagy')
  42. AnnotationURLCitation(end_index=13970, start_index=13803, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Rab%20GTPases%20play%20key%20roles,HPV%20displays%20increased%20association%20with')
  43. AnnotationURLCitation(end_index=14141, start_index=13971, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Surprisingly%2C%20excess%20GTP,distinct%20ways%20during%20intracellular%20trafficking')
  44. AnnotationURLCitation(end_index=14464, start_index=14297, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Rab%20GTPases%20play%20key%20roles,HPV%20displays%20increased%20association%20with')
  45. AnnotationURLCitation(end_index=14710, start_index=14619, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=,Rab9a')
  46. AnnotationURLCitation(end_index=14881, start_index=14711, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Surprisingly%2C%20excess%20GTP,distinct%20ways%20during%20intracellular%20trafficking')
  47. AnnotationURLCitation(end_index=15197, start_index=15060, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=the%20HPV,utilize%20the%20Rab9a%20host%20trafficking')
  48. AnnotationURLCitation(end_index=16113, start_index=15952, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=retrograde%20transport%20remains%20unclear,retrograde%20transport%20to%20the%20TGN')
  49. AnnotationURLCitation(end_index=16429, start_index=16272, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=interact%20with%20the%20dynein%20motor,retrograde%20transport%20to%20the%20TGN')
  50. AnnotationURLCitation(end_index=16726, start_index=16565, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=retrograde%20transport%20remains%20unclear,retrograde%20transport%20to%20the%20TGN')
  51. AnnotationURLCitation(end_index=17330, start_index=17196, title='TMEM9 activates Rab9-dependent alternative autophagy through interaction with Beclin1 - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/39078420/#:~:text=identified,that%20multiple%20glycosylation%20of%20TMEM9')
  52. AnnotationURLCitation(end_index=17609, start_index=17445, title='The Role of the Beclin1 Complex in Rab9-Dependent Alternative Autophagy - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12470620/#:~:text=in%20canonical%20autophagy%20and%20highlight,a%20central%20scaffold%20in%20both')
  53. AnnotationURLCitation(end_index=18798, start_index=18640, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=Rab%20proteins%20and%20their%20effectors,for%20HIV%20assembly%20and%20that')
  54. AnnotationURLCitation(end_index=18987, start_index=18799, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=insertional%20mutagenesis%2C%20we%20identified%20Rab9%2C,replication%2C%20previous%20reports%20suggested')
  55. AnnotationURLCitation(end_index=19368, start_index=19210, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=Rab%20proteins%20and%20their%20effectors,for%20HIV%20assembly%20and%20that')
  56. AnnotationURLCitation(end_index=19895, start_index=19725, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=siRNA%20showed%20the%20strongest%20effect,irrelevant%20siRNA%20control%20against%20GFP')
  57. AnnotationURLCitation(end_index=20049, start_index=19896, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=expression%20by%20%E2%88%BC80%20to%2090,to%20a%20lesser%20degree%20in')
  58. AnnotationURLCitation(end_index=20426, start_index=20256, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=siRNA%20showed%20the%20strongest%20effect,irrelevant%20siRNA%20control%20against%20GFP')
  59. AnnotationURLCitation(end_index=20580, start_index=20427, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=expression%20by%20%E2%88%BC80%20to%2090,to%20a%20lesser%20degree%20in')
  60. AnnotationURLCitation(end_index=21476, start_index=21385, title='RAB9A Plays an Oncogenic Role in Human Liver Cancer Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7210512/#:~:text=Results')
  61. AnnotationURLCitation(end_index=21801, start_index=21710, title='RAB9A Plays an Oncogenic Role in Human Liver Cancer Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7210512/#:~:text=Results')
  62. AnnotationURLCitation(end_index=22090, start_index=21921, title='RAB9A Plays an Oncogenic Role in Human Liver Cancer Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7210512/#:~:text=RAB9A%20promoted%20the%20proliferation%20and,signaling%20pathway%20in%20human%20liver')
  63. AnnotationURLCitation(end_index=23400, start_index=23242, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=The%20mutation%20or%20dysfunction%20of,By%20interacting%20with%20the%20Rab')
  64. AnnotationURLCitation(end_index=23881, start_index=23742, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=TIP47%20for%20CI,internalized%20via%20caveolae%20%20111')
  65. AnnotationURLCitation(end_index=24048, start_index=23882, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=with%20Lis1%2C%20dynein%2C%20and%20dynactin,internalized%20via%20caveolae%20%20111')
  66. AnnotationURLCitation(end_index=25156, start_index=25012, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=independent%20mannose,cargo%20trafficking%20in%20our%20cell')
  67. AnnotationURLCitation(end_index=25475, start_index=25290, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=cofractionates%20with%20endosomes%20containing%20mannose,process%20of%20transport%20vesicle%20docking')
  68. AnnotationURLCitation(end_index=26457, start_index=26325, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=NdeI%20are%20Rab9%20effectors%20,Golgi%20network')
  69. AnnotationURLCitation(end_index=26565, start_index=26458, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=mannose,Golgi%20network')
  70. AnnotationURLCitation(end_index=27137, start_index=27007, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=match%20at%20L330%20NdeI%20are,Golgi%20network')
  71. AnnotationURLCitation(end_index=27277, start_index=27138, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=TIP47%20for%20CI,internalized%20via%20caveolae%20%20111')
  72. AnnotationURLCitation(end_index=27970, start_index=27859, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=endosome%20maturation%20,23')
  73. AnnotationURLCitation(end_index=28348, start_index=28177, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=In%20addition%20to%20Rab7%2C%20late,TIP47%2C%20GCC185%2C%20p40%2C%20RUTBC1%2F2%2C%20and')
  74. AnnotationURLCitation(end_index=28472, start_index=28349, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=are%20required%20to%20transport%20CI,23')
  75. AnnotationURLCitation(end_index=28972, start_index=28803, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=different%20mechanisms%20and%20are%20present,of%20TIP47%20to%20endosomes%20containing')
  76. AnnotationURLCitation(end_index=29137, start_index=28973, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=In%20addition%20to%20Rab7%2C%20late,isoforms%2C%20Rab9A%20and%20Rab9B%2C%20which')
  77. AnnotationURLCitation(end_index=29509, start_index=29347, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=match%20at%20L321%20In%20addition,isoforms%2C%20Rab9A%20and%20Rab9B%2C%20which')
  78. AnnotationURLCitation(end_index=29649, start_index=29510, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=In%20addition%2C%20Rab9,is%20unclear%20how%20Rab7%20and')
  79. AnnotationURLCitation(end_index=29988, start_index=29874, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=Rab9%20%20,%5B90%5D%2C%20%5B91')
  80. AnnotationURLCitation(end_index=30132, start_index=29989, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=RUTBC1%20protein%2C%20a%20Rab9A%20effector,Google%20Scholar')
  81. AnnotationURLCitation(end_index=30674, start_index=30507, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Rab%20GTPases%20play%20key%20roles,HPV%20displays%20increased%20association%20with')
  82. AnnotationURLCitation(end_index=30845, start_index=30675, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Surprisingly%2C%20excess%20GTP,distinct%20ways%20during%20intracellular%20trafficking')
  83. AnnotationURLCitation(end_index=31763, start_index=31628, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=Rab4%2C%20Rab5%2C%20Rab7%2C%20Rab9%2C%20Rab10%2C,93')
  84. AnnotationURLCitation(end_index=32060, start_index=31889, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=from%20late%20endosomes%20to%20lysosomes,endosome%3B%20LE%3A%20late%20endosome%3B%20TGN')
  85. AnnotationURLCitation(end_index=32469, start_index=32353, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=share%2087%C2%A0,Golgi%20network')
  86. AnnotationURLCitation(end_index=32593, start_index=32470, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=are%20required%20to%20transport%20CI,23')
  87. AnnotationURLCitation(end_index=33502, start_index=33339, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=match%20at%20L415%20siRNA%20showed,irrelevant%20siRNA%20control%20against%20GFP')
  88. AnnotationURLCitation(end_index=33673, start_index=33503, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=siRNA%20showed%20the%20strongest%20effect,irrelevant%20siRNA%20control%20against%20GFP')
  89. AnnotationURLCitation(end_index=33972, start_index=33819, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=expression%20by%20%E2%88%BC80%20to%2090,to%20a%20lesser%20degree%20in')
  90. AnnotationURLCitation(end_index=34270, start_index=34114, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=match%20at%20L624%20measles%20virus,the%20transient%20nature%20of%20mRNA')
  91. AnnotationURLCitation(end_index=34926, start_index=34741, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=cofractionates%20with%20endosomes%20containing%20mannose,process%20of%20transport%20vesicle%20docking')
  92. AnnotationURLCitation(end_index=35535, start_index=35391, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=independent%20mannose,cargo%20trafficking%20in%20our%20cell')
  93. AnnotationURLCitation(end_index=36109, start_index=35938, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=regulate%20these%20trafficking%20steps%2C%20the,targeted%20the%20SNARE%20to%20lysosomes')
  94. AnnotationURLCitation(end_index=36246, start_index=36110, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=Rab9A,cargo%20delivery%20to%20maturing%20melanosomes')
  95. AnnotationURLCitation(end_index=36649, start_index=36478, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=regulate%20these%20trafficking%20steps%2C%20the,targeted%20the%20SNARE%20to%20lysosomes')
  96. AnnotationURLCitation(end_index=37320, start_index=37152, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=different%20mechanisms%20and%20are%20present,Rab9A%20increases%20the%20affinity%20of')
  97. AnnotationURLCitation(end_index=37537, start_index=37439, title='Ras-related protein Rab-9A | DrugBank Online', type='url_citation', url='https://go.drugbank.com/polypeptides/P51151#:~:text=Chromosome%20Location%20X')
  98. AnnotationURLCitation(end_index=37856, start_index=37734, title='RAB9A protein expression summary - The Human Protein Atlas', type='url_citation', url='https://www.proteinatlas.org/ENSG00000123595-RAB9A#:~:text=Atlas%20www,RNA%29Mouse%20brain%20Tau')
  99. AnnotationURLCitation(end_index=38294, start_index=38132, title='Ras-related protein Rab-9A | DrugBank Online', type='url_citation', url='https://go.drugbank.com/polypeptides/P51151#:~:text=binding%20protein%20homologue%20ORP1L%20interacts,Mortensen%20P%2C%20Mann%20M%3A%20Global')
  100. AnnotationURLCitation(end_index=38417, start_index=38295, title='Ras-related protein Rab-9A | DrugBank Online', type='url_citation', url='https://go.drugbank.com/polypeptides/P51151#:~:text=functional%20role%20for%20the%20GCC185,2008%20Jan')
  101. AnnotationURLCitation(end_index=38814, start_index=38656, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=Rab%20proteins%20and%20their%20effectors,for%20HIV%20assembly%20and%20that')
  102. AnnotationURLCitation(end_index=39003, start_index=38815, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=insertional%20mutagenesis%2C%20we%20identified%20Rab9%2C,replication%2C%20previous%20reports%20suggested')
  103. AnnotationURLCitation(end_index=39425, start_index=39334, title='RAB9A Plays an Oncogenic Role in Human Liver Cancer Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7210512/#:~:text=Results')
  104. AnnotationURLCitation(end_index=39796, start_index=39705, title='RAB9A Plays an Oncogenic Role in Human Liver Cancer Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC7210512/#:~:text=Results')
  105. AnnotationURLCitation(end_index=40485, start_index=40349, title='A Novel Rab9 Effector Required for Endosome-to-TGN Transport - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC2138197/#:~:text=Rab9%20GTPase%20is%20required%20for,associated%20p40')
  106. AnnotationURLCitation(end_index=40652, start_index=40520, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=NdeI%20are%20Rab9%20effectors%20,Golgi%20network')
  107. AnnotationURLCitation(end_index=40830, start_index=40711, title='Ras-related protein Rab-9A | DrugBank Online', type='url_citation', url='https://go.drugbank.com/polypeptides/P51151#:~:text=fusion%20%28By%20similarity%29,By%20similarity')
  108. AnnotationURLCitation(end_index=41034, start_index=40876, title='Rab9 GTPase Is Required for Replication of Human Immunodeficiency Virus Type 1, Filoviruses, and Measles Virus - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC1212642/#:~:text=Rab%20proteins%20and%20their%20effectors,for%20HIV%20assembly%20and%20that')
  109. AnnotationURLCitation(end_index=41263, start_index=41092, title='Rab9A is required for delivery of cargo from recycling endosomes to melanosomes - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC4690521/#:~:text=regulate%20these%20trafficking%20steps%2C%20the,targeted%20the%20SNARE%20to%20lysosomes')
  110. AnnotationURLCitation(end_index=41471, start_index=41304, title='Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC10519607/#:~:text=Rab%20GTPases%20play%20key%20roles,HPV%20displays%20increased%20association%20with')
  111. AnnotationURLCitation(end_index=41679, start_index=41518, title='Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein motor complex - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/34793709/#:~:text=retrograde%20transport%20remains%20unclear,retrograde%20transport%20to%20the%20TGN')
  112. AnnotationURLCitation(end_index=41951, start_index=41782, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=different%20mechanisms%20and%20are%20present,of%20TIP47%20to%20endosomes%20containing')
  113. AnnotationURLCitation(end_index=42091, start_index=41952, title='Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9418685/#:~:text=TIP47%20for%20CI,internalized%20via%20caveolae%20%20111')