Please use this identifier to cite or link to this item:
Title: Functional plasticity of the BNIP-2 and Cdc42GAP Homology (BCH) domain in cell signaling and cell dynamics
Authors: Pan, C.Q. 
Low, B.C. 
Keywords: BCH domain
CRAL-TRIO domain
Protein-protein interaction
Issue Date: 14-Aug-2012
Citation: Pan, C.Q., Low, B.C. (2012-08-14). Functional plasticity of the BNIP-2 and Cdc42GAP Homology (BCH) domain in cell signaling and cell dynamics. FEBS Letters 586 (17) : 2674-2691. ScholarBank@NUS Repository.
Abstract: The BNIP-2 and Cdc42GAP Homology (BCH) domains constitute a new and expanding family of highly conserved scaffold protein domains that regulate Rho, Ras and MAPK signaling, leading to cell growth, apoptosis, morphogenesis, migration and differentiation. Such versatility is achieved via their ability to target small GTPases and their immediate regulators such as GTPase-activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs), their ability to form intra-molecular or inter-molecular interaction with itself or with other BCH domains, and also by their ability to bind diverse cellular proteins such as membrane receptors, isomerase, caspases and metabolic enzymes such as glutaminase. The presence of BCH and BCH-like domains in various proteins and their divergence from the ancestral lipid-binding CRAL-TRIO domain warrant the need to examine closely their structural, functional and regulatory plasticity in isolation or in concert with other protein modules present in the same proteins. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Source Title: FEBS Letters
ISSN: 00145793
DOI: 10.1016/j.febslet.2012.04.023
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.