What is the role of Rab protein?
Rab proteins are small guanosine triphosphatases which regulate protein transport along the endocytic and exocytic pathways in all cell types. Rabs participate in vesicle budding, membrane fusion, and interactions with the cytoskeleton.
What main function do Rab small G proteins regulate?
Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled.
Where are Rab proteins found?
Rab proteins form the largest branch of the Ras superfamily of GTPases. They are localized to the cytoplasmic face of organelles and vesicles involved in the biosynthetic/secretory and endocytic pathways in eukaryotic cells.
What is the Rab cycle?
The Rab GTPase cycle. The Rab GTPase switches between GDP- and GTP-bound forms, which have different conformations. Conversion from the GDP- to the GTP-bound form is caused by nucleotide exchange, catalyzed by a GDP/GTP exchange factor (GEF).
What does a GEF do?
Guanine nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP).
How are GTPases deactivated?
Hydrolysis of GTP bound to an (active) G domain-GTPase leads to deactivation of the signaling/timer function of the enzyme. GTPase activity serves as the shutoff mechanism for the signaling roles of GTPases by returning the active, GTP-bound protein to the inactive, GDP-bound state.
What is ran GTPase?
The Ran (Ran-related or Ras-like nuclear) protein is the single member of the Ran subfamily, and the most abundant small GTPase in the cell. Like the other small GTPases, Ran functions as a molecular switch, converting between the active GTP-bound and inactive GDP-bound conformations.
What is a Rab effector?
Rab effectors, defined as proteins that interact specifically with the GTP-bound from of a Rab GTPase, come in many flavours and include molecular tethers, fusion regulators, motors, sorting adaptors, kinases, phosphatases, components of membrane contact sites and Rab regulators (Gillingham et al., 2014).
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