RAB10

RAB10 belongs to the RAS (see HRAS; MIM 190020) superfamily of small GTPases. RAB proteins localize to exocytic and endocytic compartments and regulate intracellular vesicle trafficking (Bao et al., 1998 [PubMed 9918381]).[supplied by OMIM, Mar 2009]

RAB10, Member RAS Oncogene Family

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21248164).
Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:21248164).
That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane (PubMed:21248164).
Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane (By similarity).
In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response (By similarity).
Also plays a specific role in asymmetric protein transport to the plasma membrane (PubMed:16641372).
In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane (By similarity).
In epithelial cells, it regulates transport from the Golgi to the basolateral membrane (PubMed:16641372).
May play a role in the basolateral recycling pathway and in phagosome maturation (By similarity).
May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion (PubMed:23263280).
Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis (PubMed:30398148).
When phosphorylated by LRRK2 on Thr-73, binds RILPL1 and inhibits ciliogenesis (PubMed:30398148).By Similarity4 Publications
(Microbial infection) Upon Legionella pneumophila infection promotes endoplasmic reticulum recruitment and bacterial replication. Plays a role in remodeling the Legionella-containing vacuole (LCV) into an endoplasmic reticulum-like vacuole.

Biological Process antigen processing and presentationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process axonogenesisISS:UniProtKB
Biological Process cellular response to insulin stimulusISS:UniProtKB
Biological Process endoplasmic reticulum tubular network organizationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process endosomal transportManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process establishment of neuroblast polarityISS:UniProtKB
Biological Process establishment of protein localization to endoplasmic reticulum membraneManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process establishment of protein localization to membraneManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process Golgi to plasma membrane protein transportISS:UniProtKB
Biological Process Golgi to plasma membrane transportISS:UniProtKB
Biological Process polarized epithelial cell differentiationISS:UniProtKB
Biological Process protein localization to basolateral plasma membraneISS:UniProtKB
Biological Process protein localization to plasma membraneISS:UniProtKB
Biological Process protein secretionManual Assertion Based On ExperimentIBA:GO_Central
Biological Process regulated exocytosisManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of exocytosisManual Assertion Based On ExperimentIBA:GO_Central
Biological Process vesicle docking involved in exocytosisManual Assertion Based On ExperimentIBA:GO_Central
Biological Process vesicle-mediated transportISS:UniProtKB

Cytoplasmic vesicle membrane
Golgi apparatus membrane
Golgi apparatus, trans-Golgi network membrane
Endosome membrane
Recycling endosome membrane
Cytoplasmic vesicle, phagosome membrane
Cytoplasm, cytoskeleton, cilium basal body
Endoplasmic reticulum membrane
Cytoplasm, perinuclear region
Associates with SLC2A4/GLUT4 storage vesicles (PubMed:22908308).
Localizes to the base of the cilium when phosphorylated by LRRK2 on Thr-73 (PubMed:20576682, PubMed:30398148).
Transiently associates with phagosomes (By similarity).
Localizes to the endoplasmic reticulum at domains of new tubule growth (PubMed:23263280).

Ubiquitinated upon Legionella pneumophila infection. Ubiquitination does not lead to proteasomal degradation.
Phosphorylation of Thr-73 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.