Please use this identifier to cite or link to this item: https://doi.org/10.1038/sj.onc.1209274
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dc.titleBNIP-Sα induces cell rounding and apoptosis by displacing p50RhoGAP and facilitating RhoA activation via its unique motifs in the BNIP-2 and Cdc42GAP homology domain
dc.contributor.authorZhou, Y.T.
dc.contributor.authorGuy, G.R.
dc.contributor.authorLow, B.C.
dc.date.accessioned2014-10-27T08:22:59Z
dc.date.available2014-10-27T08:22:59Z
dc.date.issued2006-04-13
dc.identifier.citationZhou, Y.T., Guy, G.R., Low, B.C. (2006-04-13). BNIP-Sα induces cell rounding and apoptosis by displacing p50RhoGAP and facilitating RhoA activation via its unique motifs in the BNIP-2 and Cdc42GAP homology domain. Oncogene 25 (16) : 2393-2408. ScholarBank@NUS Repository. https://doi.org/10.1038/sj.onc.1209274
dc.identifier.issn09509232
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100185
dc.description.abstractChanges in cell morphology are linked to many cellular events including cytokinesis, differentiation, migration and apoptosis. We recently showed that BNIP-Sα induced cell rounding that leads to apoptosis via its BNIP-2 and Cdc42GAP Homology (BCH) domain, but the underlying mechanism has not been determined. Here, we have identified a unique region (amino acid 133-177) of the BNIP-Sα BCH domain that targets RhoA, but not Cdc42 or Rac1 and only the dominant-negative form of RhoA could prevent the resultant cell rounding and apoptotic effect. The RhoA-binding region consists of two parts; one region (residues 133-147) that shows some homology to part of the RhoA switch I region and an adjacent sequence (residues 148-177) that resembles the REM class I RhoA-binding motif. The sequence 133-147 is also necessary for its heterophilic interaction with the BCH domain of the Rho GTPase-activating protein, p50RhoGAP/ Cdc42GAP. These overlapping motifs allow tripartite competition such that overexpression of BNIP-Sα could reduce p50RhoGAP binding to RhoA and restore RhoA activation. Furthermore, BNIP-Sα mutants lacking the RhoA-binding motif completely failed to induce cell rounding and apoptosis. Therefore, via unique binding motifs within its BCH domain, BNIP-Sα could interact and activate RhoA while preventing its inhibition by p50RhoGAP. This concerted mechanism could allow effective propagation of the RhoA pathway for cell rounding and apoptosis. © 2006 Nature Publishing Group All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/sj.onc.1209274
dc.sourceScopus
dc.subjectApoptosis
dc.subjectBCH domain
dc.subjectBNIP-S
dc.subjectCell founding
dc.subjectp50RhoGAP/Cdc42GAP
dc.subjectRhoA
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1038/sj.onc.1209274
dc.description.sourcetitleOncogene
dc.description.volume25
dc.description.issue16
dc.description.page2393-2408
dc.description.codenONCNE
dc.identifier.isiut000236764300011
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