RALA Antibody - #DF7958

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. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody.

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

Cell membrane>Lipid-anchor>Cytoplasmic side. Cleavage furrow. Midbody>Midbody ring.
Note: Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles (PubMed:19306925). May colocalize with CNTRL/centriolin at the midbody ring (PubMed:16213214). However, localization at the midbody at late cytokinesis was not confirmed (PubMed:18756269).

Interacts (via effector domain) with RALBP1. Interacts with EXOC2/Sec5 and EXOC8/Exo84; binding to EXOC2 and EXOC8 is mutually exclusive. Interacts with Clostridium exoenzyme C3. Interacts with RALGPS1. Interacts with LPAR1 and LPAR2. Interacts with GRK2 in response to LPAR1 activation. RALA and GRK2 binding to LPAR1 is mutually exclusive. Interacts with CDC42 (By similarity).

Belongs to the small GTPase superfamily. Ras family.