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]

Full Name

RAB10, Member RAS Oncogene Family

Function

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

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

Cellular Location

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).

PTM

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.