Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0033863
Title: Cross-species analyses identify the BNIP-2 and Cdc42gap Homology (BCH) domain as a distinct functional subclass of the CRAL_TRIO/sec14 superfamily
Authors: Gupta, A.B.
Wee, L.E.
Zhou, Y.T. 
Hortsch, M.
Low, B.C. 
Issue Date: 27-Mar-2012
Citation: Gupta, A.B., Wee, L.E., Zhou, Y.T., Hortsch, M., Low, B.C. (2012-03-27). Cross-species analyses identify the BNIP-2 and Cdc42gap Homology (BCH) domain as a distinct functional subclass of the CRAL_TRIO/sec14 superfamily. PLoS ONE 7 (3) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0033863
Abstract: The CRAL_TRIO protein domain, which is unique to the Sec14 protein superfamily, binds to a diverse set of small lipophilic ligands. Similar domains are found in a range of different proteins including neurofibromatosis type-1, a Ras GTPase-activating Protein (RasGAP) and Rho guanine nucleotide exchange factors (RhoGEFs). Proteins containing this structural protein domain exhibit a low sequence similarity and ligand specificity while maintaining an overall characteristic three-dimensional structure. We have previously demonstrated that the BNIP-2 and Cdc42GAP Homology (BCH) protein domain, which shares a low sequence homology with the CRAL_TRIO domain, can serve as a regulatory scaffold that binds to Rho, RhoGEFs and RhoGAPs to control various cell signalling processes. In this work, we investigate 175 BCH domain-containing proteins from a wide range of different organisms. A phylogenetic analysis with ~100 CRAL_TRIO and similar domains from eight representative species indicates a clear distinction of BCH-containing proteins as a novel subclass within the CRAL_TRIO/Sec14 superfamily. BCH-containing proteins contain a hallmark sequence motif R(R/K)h(R/K)(R/K)NL(R/K)xhhhhHPs ('h' is large and hydrophobic residue and 's' is small and weekly polar residue) and can be further subdivided into three unique subtypes associated with BNIP-2-N, macro- and RhoGAP-type protein domains. A previously unknown group of genes encoding 'BCH-only' domains is also identified in plants and arthropod species. Based on an analysis of their gene-structure and their protein domain context we hypothesize that BCH domain-containing genes evolved through gene duplication, intron insertions and domain swapping events. Furthermore, we explore the point of divergence between BCH and CRAL-TRIO proteins in relation to their ability to bind small GTPases, GAPs and GEFs and lipid ligands. Our study suggests a need for a more extensive analysis of previously uncharacterized BCH, 'BCH-like' and CRAL_TRIO-containing proteins and their significance in regulating signaling events involving small GTPases. © 2012 Gupta et al.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/109277
ISSN: 19326203
DOI: 10.1371/journal.pone.0033863
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