RIC, a calmodulin-binding Ras-like GTPase

TitleRIC, a calmodulin-binding Ras-like GTPase
Publication TypeJournal Article
Year of Publication1996
AuthorsWes PD, Yu M, Montell C
JournalEMBO J
Volume15
Pagination5839-48
Date Published1996 Nov 1
ISSN0261-4189
KeywordsAmino Acid Sequence, Animals, Animals, Genetically Modified, Base Sequence, Brain, Calmodulin-Binding Proteins, Cloning, Molecular, Conserved Sequence, DNA Primers, Drosophila, GTP Phosphohydrolases, Humans, Molecular Sequence Data, Monomeric GTP-Binding Proteins, Neurons, ras Proteins, Sequence Homology, Amino Acid, Signal Transduction
Abstract

Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. In a screen for calmodulin-binding proteins, we identified RIC, a protein related to the Ras subfamily of small GTPases. In addition to the ability to bind calmodulin, a number of unique features distinguished RIC from other Ras-like GTPases, including the absence of a signal for prenylation and a distinct effector (G2) domain. Furthermore, we describe two human proteins, RIN and RIT, which were 71% and 66% identical to RIC respectively, shared related G2 domains with RIC, and lacked prenylation signals, suggesting that the RIC family is conserved from flies to humans. While Ric and RIT were widely expressed, expression of RIN was confined to the neuron system.

Alternate JournalEMBO J.
PubMed ID8918462
PubMed Central IDPMC452332
Grant ListEY08177 / EY / NEI NIH HHS / United States