RALA

The product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins. [provided by RefSeq, Jul 2008]

RAS Like Proto-Oncogene A

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 (PubMed:18756269, PubMed:19306925, PubMed:20005108, PubMed:21822277, PubMed:30500825).
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 (PubMed:20005108).
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 (PubMed:19306925).
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 (PubMed:18756269).
During mitosis, also controls mitochondrial fission by recruiting to the mitochondrion RALBP1, which mediates the phosphorylation and activation of DNM1L by the mitotic kinase cyclin B-CDK1 (PubMed:21822277).

Biological Process actin cytoskeleton reorganizationManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process cell cycleIEA:UniProtKB-KW
Biological Process cell divisionIEA:UniProtKB-KW
Biological Process chemotaxisManual Assertion Based On ExperimentTAS:ProtInc
Biological Process establishment of protein localization to mitochondrionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process exocytosisIEA:UniProtKB-KW
Biological Process membrane raft localizationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process neural tube closureIEA:Ensembl
Biological Process positive regulation of filopodium assemblyManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process positive regulation of mitochondrial fissionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process Ras protein signal transductionManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of exocytosisManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process signal transductionManual Assertion Based On ExperimentTAS:ProtInc

Cell membrane
Cleavage furrow
Midbody, Midbody ring
Mitochondrion
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).
Relocalizes to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277).

Hiatt-Neu-Cooper neurodevelopmental syndrome (HINCONS):
An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, delayed walking or inability to walk, impaired intellectual development, poor or absent speech, axial hypotonia, and facial dysmorphism. Additional variable features may include seizures, autistic or behavioral abnormalities, and brain abnormalities.

Phosphorylated. Phosphorylation at Ser-194 by AURKA/Aurora kinase A, during mitosis, induces RALA localization to the mitochondrion where it regulates mitochondrial fission.
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).
(Microbial infection) Glucosylated at Thr-46 by P.sordellii toxin TcsL from strain 6018 (PubMed:8858106).
Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form (PubMed:8858106).
Not glucosylated by TcsL from strain VPI 9048 (PubMed:8858106).