Cytokinesis and cancer:Polo loves ROCK'n' Rho(A)

查看全文 作　　者：Jing Li Jue Wang Hong Jiao Ji Liao Xingzhi [1]Xu

机构地区：[1]Laboratory of Cancer Biology, College of Life Science, Capital Normal University, Beijing 100048, China

出　　处：《Journal of Genetics and Genomics》索引2010年第37卷第3期,共14页

基　　金：supported by the National Natural Science Foundation of China (NSFC) (No.30700420);Beijing Nova Program (No.2007B062);Scientific Research Program of Beijing Municipal Commission of Education (No.KM200810028013);Scientific Research Foundation for the Returned Overseas Chinese Scholars from Beijing Municipal Commission of Human Resources (No.085402600);from State Education Ministry (SRF for ROCS,SEM) to J.L.X.X.was supported by the startup fund from CNU,NSFC funds (No.30570371,90608014,and 30711120570);the Program for New Century Excellent Talents in University (No.NCET-06-0187);Beijing Natural Science Foundation Program and Scientific Research Key Program of Beijing Municipal Commission of Education (No.KZ200810028014);Funding Project for Academic Human Resources Development in Institutions of Higher Learning Under the Jurisdiction of Beijing Municipality (PHR(IHLB)) 摘　　要：Cytokinesis is the last step of the M (mitosis) phase, yet it is crucial for the faithful division of one cell into two. Cytokinesis failure is often associated with cancer. Cytokinesis can be morphologically divided into four steps: cleavage furrow initiation, cleavage furrow ingression, midbody formation and abscission. Molecular studies have revealed that RhoA as well as its regulators and effectors are important players to ensure a successful cytokinesis. At the same time, Polo-like kinase 1 (Plk1) is an important kinase that can target many substrates and carry out different functions during mitosis, including cytokinesis. Recent studies are beginning to unveil a closer tie between Plk1 and RhoA networks. More specifically, Plk1 phosphorylates the centralspindlin complex Cyk4 and MKLP1/CHO1, thus recruiting RhoA guanine nucleotide-exchange factor (GEF) Ect2 through its phosphopeptide-binding BRCT domains. Ect2 itself can be phosphorylated by Plk1 in vitro. Plk1 can also phosphorylate another GEF MyoGEF to regulate RhoA activity. Once activated, RhoA-GTP will activate downstream effectors, including ROCK1 and ROCK2. ROCK2 is among the proteins that associate with Plk1 Polo-binding domain (PBD) in a large proteomic screen, and Plk1 can phosphorylate ROCK2 in vitro. We review current understandings of the interplay between Plk1, RhoA proteins and other proteins (e.g., NudC, MKLP2, PRC1, CEP55) involved in cytokinesis, with particular emphasis of its clinical implications in cancer. 关键词：胞质分裂癌症磷酸化作用有丝分裂过程蛋白质相互作用细胞分裂鸟嘌呤核苷酸蛋白激酶

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Cytokinesis and cancer:Polo loves ROCK'n' Rho(A)

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