RAB1A Antibody - #DF9817

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport.

Phosphorylated by CDK1 kinase during mitosis.

Phosphocholinated at Ser-79 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI). Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring accessibility to L.pneumophila GTPase effector LepB.

Golgi apparatus. Endoplasmic reticulum. Early endosome. Cytoplasm>Cytosol. Membrane. Melanosome.
Note: Alternates between membrane-associated and cytosolic forms.

May interact with YIPF5 (By similarity). Interacts with C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1 kinase complex. Interacts with GDI1; this promotes dissociation from membranes.

(Microbial infection) Interacts with L.pneumophila AnkX.

(Microbial infection) Interacts with L.pneumophila Lem3.

(Microbial infection) Interacts with L.pneumophila LidA.

(Microbial infection) Interacts with L.pneumophila DrrA; this disrupts the interaction between RAB1A and GDI1 and promotes the exchange of RAB1A-bound GDP with GTP.

(Microbial infection) Interacts with E.coli EspG and S.flexneri VirA; this impairs ER to Golgi trafficking and protein secretion.

(Microbial infection) Interacts with L.pneumophila and L.drancourtii LepB; this enhances RAB1A GTPase activity.

(Microbial infection) Identified in a complex composed of RAB1A, ARF6 and E.coli EspG.

Belongs to the small GTPase superfamily. Rab family.