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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Rho GTPase activating protein 33

This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. Alternative splice variants encoding different isoforms have been identified in this gene. [provided by RefSeq, Feb 2010] (from NCBI)
Top mentioned proteins: GAP, Cdc42, CAN, RhoGAP, ACID
Papers on NOMA-GAP
NOMA-GAP/ARHGAP33 regulates synapse development and autistic-like behavior in the mouse.
Rosário et al., Berlin, Germany. In Mol Psychiatry, Sep 2015
Here we show, using genetically engineered mice, that the Cdc42 GTPase-activating multiadaptor protein, NOMA-GAP, regulates autism-like social behavior in the mouse, as well as dendritic spine and synapse development.
Neocortical dendritic complexity is controlled during development by NOMA-GAP-dependent inhibition of Cdc42 and activation of cofilin.
Birchmeier et al., Berlin, Germany. In Genes Dev, 2012
By generating genetically modified mice, we demonstrate that this is catalyzed in vivo by the novel Cdc42-GAP NOMA-GAP.
Regulation of dendritic branching by Cdc42 GAPs.
Cooper et al., Seattle, United States. In Genes Dev, 2012
1743-1757) shows that a Cdc42-specific GTPase-activating protein (NOMA-GAP) regulates the branching of dendrites by neurons in the top layers of the mouse cortex.
The neurite outgrowth multiadaptor RhoGAP, NOMA-GAP, regulates neurite extension through SHP2 and Cdc42.
Birchmeier et al., Berlin, Germany. In J Cell Biol, 2007
Results show that neurite outgrowth multiadaptor RhoGAP protein, NOMA-GAP, plays an essential role downstream of NGF in promoting neurite outgrowth and extension by recruiting SHP2 and activating Cdc42.
Physical and functional interaction of Fyn tyrosine kinase with a brain-enriched Rho GTPase-activating protein TCGAP.
Yamamoto et al., Tokyo, Japan. In J Biol Chem, 2006
TCGAP interacts with Fyn and is phosphorylated by Fyn, with tyrosine-406 in the GTPase-activating protein (GAP) domain as a major Fyn-mediated phosphorylation site.
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