التفاصيل البيبلوغرافية
| العنوان: |
Cross-Species Analyses Identify the BNIP-2 and Cdc42GAP Homology (BCH) Domain as a Distinct Functional Subclass of the CRALTRIO/Sec14 Superfamily. |
| المؤلفون: |
Gupta, Anjali Bansal, Wee, Liang En, Yi Ting Zhou, Hortsch, Michael, Boon Chuan Low |
| المصدر: |
PLoS ONE; Mar2012, Vol. 7 Issue 3, p1-13, 13p |
| مصطلحات موضوعية: |
PROTEINS, NEUROFIBROMATOSIS, CYTOSKELETAL proteins, MEDICAL research, DRUG lipophilicity |
| مستخلص: |
The CRALTRIO 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 GTPaseactivating 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 threedimensional structure. We have previously demonstrated that the BNIP-2 and Cdc42GAP Homology (BCH) protein domain, which shares a low sequence homology with the CRALTRIO 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 CRALTRIO and similar domains from eight representative species indicates a clear distinction of BCH-containing proteins as a novel subclass within the CRALTRIO/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 CRALTRIO-containing proteins and their significance in regulating signaling events involving small GTPases. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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