RAL B Human Recombinant Protein

Function: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. Ref.12

Enzyme regulation: Alternate between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).

Subunit structure: Interacts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain. Ref.9 Ref.10 Ref.14

Subcellular location: Cell membrane; Lipid-anchor; Cytoplasmic side. Note: During late cytokinesis localizes at the midbody. Ref.11 Ref.12

Post-translational modification: Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).

Sequence similarities: Belongs to the small GTPase superfamily. Ras family.