dc.contributor.author | Wang, Yang | |
dc.contributor.author | Azuma, Yoshiaki | |
dc.contributor.author | Moore, David S. | |
dc.contributor.author | Osheroff, Neil | |
dc.contributor.author | Neufeld, Kristi L. | |
dc.date.accessioned | 2014-10-07T18:45:45Z | |
dc.date.available | 2014-10-07T18:45:45Z | |
dc.date.issued | 2008-10-01 | |
dc.identifier.citation | Wang, Yang et al. (2008). "Interaction between Tumor Suppressor Adenomatous Polyposis Coli and Topoisomerase IIα: Implication for the G2/M Transition." Molecular Biology of the Cell, 19(10):4076-86. http://www.dx.doi.org/10.1091/mbc.E07-12-1296 | |
dc.identifier.issn | 1059-1524 | |
dc.identifier.uri | http://hdl.handle.net/1808/15209 | |
dc.description | This is the publisher's version, also available electronically from http://www.molbiolcell.org/content/19/10/4076 | |
dc.description.abstract | The tumor suppressor adenomatous polyposis coli (APC) is implicated in regulating multiple stages of the cell cycle. APC participation in G1/S is attributed to its recognized role in Wnt signaling. APC function in the G2/M transition is less well established. To identify novel protein partners of APC that regulate the G2/M transition, APC was immunoprecipitated from colon cell lysates and associated proteins were analyzed by matrix-assisted laser desorption ionization/time of flight (MALDI-TOF). Topoisomerase IIα (topo IIα) was identified as a potential binding partner of APC. Topo IIα is a critical regulator of G2/M transition. Evidence supporting an interaction between endogenous APC and topo IIα was obtained by coimmunoprecipitation, colocalization, and Förster resonance energy transfer (FRET). The 15-amino acid repeat region of APC (M2-APC) interacted with topo IIα when expressed as a green fluorescent protein (GFP)-fusion protein in vivo. Although lacking defined nuclear localization signals (NLS) M2-APC predominantly localized to the nucleus. Furthermore, cells expressing M2-APC displayed condensed or fragmented nuclei, and they were arrested in the G2 phase of the cell cycle. Although M2-APC contains a β-catenin binding domain, biochemical studies failed to implicate β-catenin in the observed phenotype. Finally, purified recombinant M2-APC enhanced topo IIα activity in vitro. Together, these data support a novel role for APC in the G2/M transition, potentially through association with topo IIα. | |
dc.publisher | American Society for Cell Biology | |
dc.title | Interaction between Tumor Suppressor Adenomatous Polyposis Coli and Topoisomerase IIα: Implication for the G2/M Transition | |
dc.type | Article | |
kusw.kuauthor | Wang, Yang | |
kusw.kuauthor | Azuma, Yoshiaki | |
kusw.kuauthor | Neufeld, Kristi L. | |
kusw.kudepartment | Molecular Biosciences | |
kusw.oastatus | fullparticipation | |
dc.identifier.doi | 10.1091/mbc.E07-12-1296 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess | |