cross-species analyses identify the bnip-2 and cdc42gap homology (bch) domain as a distinct functional subclass of the cral_triosec14 superfamily跨物种分析识别bnip-2和cdc42gap同源性(bch)域作为一种独特的功能的子类cral_triosec14总科.pdfVIP

Cross-Species Analyses Identify the BNIP-2 and Cdc42GAP Homology (BCH) Domain as a Distinct Functional Subclass of the CRAL_TRIO/Sec14 Superfamily 1,2 1 1¤ 3 1,2 Anjali Bansal Gupta , Liang En Wee , Yi Ting Zhou , Michael Hortsch , Boon Chuan Low * 1 Department of Biological Sciences, National University of Singapore, Singapore, Singapore, 2 Mechanobiology Institute, National University of Singapore, Singapore, Singapore, 3 Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America 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