메뉴 건너뛰기




Volumn 43, Issue 1, 2011, Pages 120-129

Calcium- and integrin-binding protein 1 regulates microtubule organization and centrosome segregation through polo like kinase 3 during cell cycle progression

Author keywords

Centrosomes; CIB1; Cytokinesis; Microtubules; Multinucleation; Plk3; T47D

Indexed keywords

BINDING PROTEIN; CALCIUM AND INTEGRIN BINDING PROTEIN 1; POLO LIKE KINASE 2; POLO LIKE KINASE 3; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG;

EID: 78650251404     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.10.003     Document Type: Article
Times cited : (19)

References (37)
  • 1
    • 62849123093 scopus 로고    scopus 로고
    • Polo-like kinases: Conservation and divergence in their functions and regulation
    • V. Archambault, and D.M. Glover Polo-like kinases: conservation and divergence in their functions and regulation Nat Rev Mol Cell Biol 10 2009 265 275
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 265-275
    • Archambault, V.1    Glover, D.M.2
  • 2
    • 0037179845 scopus 로고    scopus 로고
    • Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways
    • M. Bahassi el, C.W. Conn, D.L. Myer, R.F. Hennigan, C.H. McGowan, and Y. Sanchez Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways Oncogene 21 2002 6633 6640
    • (2002) Oncogene , vol.21 , pp. 6633-6640
    • Bahassi El, M.1    Conn, C.W.2    Myer, D.L.3    Hennigan, R.F.4    McGowan, C.H.5    Sanchez, Y.6
  • 3
    • 0027178446 scopus 로고
    • Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila
    • F.J. Clay, S.J. McEwen, I. Bertoncello, A.F. Wilks, and A.R. Dunn Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila Proc Natl Acad Sci USA 90 1993 4882 4886
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4882-4886
    • Clay, F.J.1    McEwen, S.J.2    Bertoncello, I.3    Wilks, A.F.4    Dunn, A.R.5
  • 4
    • 0034671732 scopus 로고    scopus 로고
    • Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3
    • C.W. Conn, R.F. Hennigan, W. Dai, Y. Sanchez, and P.J. Stambrook Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3 Cancer Res 60 2000 6826 6831
    • (2000) Cancer Res , vol.60 , pp. 6826-6831
    • Conn, C.W.1    Hennigan, R.F.2    Dai, W.3    Sanchez, Y.4    Stambrook, P.J.5
  • 5
    • 18844396190 scopus 로고    scopus 로고
    • Cleavage furrow formation and ingression during animal cytokinesis: A microtubule legacy
    • P.P. D'Avino, M.S. Savoian, and D.M. Glover Cleavage furrow formation and ingression during animal cytokinesis: a microtubule legacy J Cell Sci 118 2005 1549 1558
    • (2005) J Cell Sci , vol.118 , pp. 1549-1558
    • D'Avino, P.P.1    Savoian, M.S.2    Glover, D.M.3
  • 6
    • 0036134506 scopus 로고    scopus 로고
    • Down-regulation of PLK3 gene expression by types and amount of dietary fat in rat colon tumors
    • W. Dai, T. Liu, Q. Wang, C.V. Rao, and B.S. Reddy Down-regulation of PLK3 gene expression by types and amount of dietary fat in rat colon tumors Int J Oncol 20 2002 121 126
    • (2002) Int J Oncol , vol.20 , pp. 121-126
    • Dai, W.1    Liu, T.2    Wang, Q.3    Rao, C.V.4    Reddy, B.S.5
  • 7
    • 0037048294 scopus 로고    scopus 로고
    • Polo-like kinases and centrosome regulation
    • W. Dai, Q. Wang, and F. Traganos Polo-like kinases and centrosome regulation Oncogene 21 2002 6195 6200
    • (2002) Oncogene , vol.21 , pp. 6195-6200
    • Dai, W.1    Wang, Q.2    Traganos, F.3
  • 8
    • 0035462382 scopus 로고    scopus 로고
    • Re-evaluating centrosome function
    • S. Doxsey Re-evaluating centrosome function Nat Rev Mol Cell Biol 2 2001 688 698
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 688-698
    • Doxsey, S.1
  • 9
    • 13244269808 scopus 로고    scopus 로고
    • Polo-like kinases and oncogenesis
    • F. Eckerdt, J. Yuan, and K. Strebhardt Polo-like kinases and oncogenesis Oncogene 24 2005 267 276
    • (2005) Oncogene , vol.24 , pp. 267-276
    • Eckerdt, F.1    Yuan, J.2    Strebhardt, K.3
  • 10
    • 10744221449 scopus 로고    scopus 로고
    • The molecular basis for phosphodependent substrate targeting and regulation of plks by the polo-box domain
    • A.E. Elia, P. Rellos, L.F. Haire, J.W. Chao, F.J. Ivins, and K. Hoepker The molecular basis for phosphodependent substrate targeting and regulation of plks by the polo-box domain Cell 115 2003 83 95
    • (2003) Cell , vol.115 , pp. 83-95
    • Elia, A.E.1    Rellos, P.2    Haire, L.F.3    Chao, J.W.4    Ivins, F.J.5    Hoepker, K.6
  • 11
    • 0028336680 scopus 로고
    • Sak, a murine protein-serine/threonine kinase that is related to the Drosophila polo kinase and involved in cell proliferation
    • C. Fode, B. Motro, S. Yousefi, M. Heffernan, and J.W. Dennis Sak, a murine protein-serine/threonine kinase that is related to the Drosophila polo kinase and involved in cell proliferation Proc Natl Acad Sci U S A 91 1994 6388 6392
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6388-6392
    • Fode, C.1    Motro, B.2    Yousefi, S.3    Heffernan, M.4    Dennis, J.W.5
  • 12
    • 0034609729 scopus 로고    scopus 로고
    • Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages
    • U. Holtrich, G. Wolf, J. Yuan, J. Bereiter-Hahn, T. Karn, and M. Weiler Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages Oncogene 19 2000 4832 4839
    • (2000) Oncogene , vol.19 , pp. 4832-4839
    • Holtrich, U.1    Wolf, G.2    Yuan, J.3    Bereiter-Hahn, J.4    Karn, T.5    Weiler, M.6
  • 13
    • 13144249168 scopus 로고    scopus 로고
    • Physical and functional interactions between mitotic kinases during polyploidization and megakaryocytic differentiation
    • X. Huang, Q. Ruan, Y. Fang, F. Traganos, Z. Darzynkiewicz, and W. Dai Physical and functional interactions between mitotic kinases during polyploidization and megakaryocytic differentiation Cell Cycle 3 2004 946 951
    • (2004) Cell Cycle , vol.3 , pp. 946-951
    • Huang, X.1    Ruan, Q.2    Fang, Y.3    Traganos, F.4    Darzynkiewicz, Z.5    Dai, W.6
  • 14
    • 13044313478 scopus 로고    scopus 로고
    • The polo-like protein kinases Fnk and Snk associate with a Ca (2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity
    • G. Kauselmann, M. Weiler, P. Wulff, S. Jessberger, U. Konietzko, and J. Scafidi The polo-like protein kinases Fnk and Snk associate with a Ca (2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity Embo J 18 1999 5528 5539
    • (1999) Embo J , vol.18 , pp. 5528-5539
    • Kauselmann, G.1    Weiler, M.2    Wulff, P.3    Jessberger, S.4    Konietzko, U.5    Scafidi, J.6
  • 15
    • 0028918625 scopus 로고
    • Alteration of collagen-dependent adhesion, motility, and morphogenesis by the expression of antisense alpha 2 integrin mRNA in mammary cells
    • P.J. Keely, A.M. Fong, M.M. Zutter, and S.A. Santoro Alteration of collagen-dependent adhesion, motility, and morphogenesis by the expression of antisense alpha 2 integrin mRNA in mammary cells J Cell Sci 108 1995 595 607
    • (1995) J Cell Sci , vol.108 , pp. 595-607
    • Keely, P.J.1    Fong, A.M.2    Zutter, M.M.3    Santoro, S.A.4
  • 16
    • 0032482986 scopus 로고    scopus 로고
    • Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk
    • K.S. Lee, T.Z. Grenfell, F.R. Yarm, and R.L. Erikson Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk Proc Natl Acad Sci USA 95 1998 9301 9306
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9301-9306
    • Lee, K.S.1    Grenfell, T.Z.2    Yarm, F.R.3    Erikson, R.L.4
  • 17
    • 0029770725 scopus 로고    scopus 로고
    • Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas
    • B. Li, B. Ouyang, H. Pan, P.T. Reissmann, D.J. Slamon, and R. Arceci Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas J Biol Chem 271 1996 19402 19408
    • (1996) J Biol Chem , vol.271 , pp. 19402-19408
    • Li, B.1    Ouyang, B.2    Pan, H.3    Reissmann, P.T.4    Slamon, D.J.5    Arceci, R.6
  • 18
    • 0037359602 scopus 로고    scopus 로고
    • The serum-inducible protein kinase snk is a G(1) phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB
    • S. Ma, M.A. Liu, Y.L. Yuan, and R.L. Erikson The serum-inducible protein kinase snk is a G(1) phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB Mol Cancer Res 1 2003 376 384
    • (2003) Mol Cancer Res , vol.1 , pp. 376-384
    • Ma, S.1    Liu, M.A.2    Yuan, Y.L.3    Erikson, R.L.4
  • 19
    • 0033145516 scopus 로고    scopus 로고
    • Centrosome duplication in mammalian somatic cells requires E2F and Cdk2-cyclin A
    • P. Meraldi, J. Lukas, A.M. Fry, J. Bartek, and E.A. Nigg Centrosome duplication in mammalian somatic cells requires E2F and Cdk2-cyclin A Nat Cell Biol 1 1999 88 93
    • (1999) Nat Cell Biol , vol.1 , pp. 88-93
    • Meraldi, P.1    Lukas, J.2    Fry, A.M.3    Bartek, J.4    Nigg, E.A.5
  • 20
    • 34848852678 scopus 로고    scopus 로고
    • Alpha-actinin is required for tightly regulated remodeling of the actin cortical network during cytokinesis
    • S. Mukhina, Y.L. Wang, and M. Murata-Hori Alpha-actinin is required for tightly regulated remodeling of the actin cortical network during cytokinesis Dev Cell 13 2007 554 565
    • (2007) Dev Cell , vol.13 , pp. 554-565
    • Mukhina, S.1    Wang, Y.L.2    Murata-Hori, M.3
  • 21
    • 42049113615 scopus 로고    scopus 로고
    • Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion
    • M.U. Naik, T.U. Naik, A.T. Suckow, M.K. Duncan, and U.P. Naik Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion Cancer Res 68 2008 2194 2203
    • (2008) Cancer Res , vol.68 , pp. 2194-2203
    • Naik, M.U.1    Naik, T.U.2    Suckow, A.T.3    Duncan, M.K.4    Naik, U.P.5
  • 22
    • 0242579243 scopus 로고    scopus 로고
    • Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen
    • M.U. Naik, and U.P. Naik Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen Blood 102 2003 3629 3636
    • (2003) Blood , vol.102 , pp. 3629-3636
    • Naik, M.U.1    Naik, U.P.2
  • 23
    • 77955369977 scopus 로고    scopus 로고
    • Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells
    • M.U. Naik, N.T. Pham, K. Beebe, W. Dai, and Naik UP Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells Int J Cancer 2010 [Epub ahead of print]
    • (2010) Int J Cancer
    • Naik, M.U.1    Pham, N.T.2    Beebe, K.3    Dai, W.4    Naik, U.P.5
  • 24
    • 0043240190 scopus 로고    scopus 로고
    • Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen
    • U.P. Naik, and M.U. Naik Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen Blood 102 2003 1355 1362
    • (2003) Blood , vol.102 , pp. 1355-1362
    • Naik, U.P.1    Naik, M.U.2
  • 25
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain
    • U.P. Naik, P.M. Patel, and L.V. Parise Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain J Biol Chem 272 1997 4651 4654
    • (1997) J Biol Chem , vol.272 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 26
    • 0038492408 scopus 로고    scopus 로고
    • Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate
    • H. Nakajima, F. Toyoshima-Morimoto, E. Taniguchi, and E. Nishida Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate J Biol Chem 278 2003 25277 25280
    • (2003) J Biol Chem , vol.278 , pp. 25277-25280
    • Nakajima, H.1    Toyoshima-Morimoto, F.2    Taniguchi, E.3    Nishida, E.4
  • 27
    • 0030695943 scopus 로고    scopus 로고
    • Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions
    • B. Ouyang, H. Pan, L. Lu, J. Li, P. Stambrook, and B. Li Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions J Biol Chem 272 1997 28646 28651
    • (1997) J Biol Chem , vol.272 , pp. 28646-28651
    • Ouyang, B.1    Pan, H.2    Lu, L.3    Li, J.4    Stambrook, P.5    Li, B.6
  • 29
    • 0027460208 scopus 로고
    • Growth arrest of the breast cancer cell line, T47D, by TNF alpha; Cell cycle specificity and signal transduction
    • L. Pusztai, C.E. Lewis, and J.O. McGee Growth arrest of the breast cancer cell line, T47D, by TNF alpha; cell cycle specificity and signal transduction Br J Cancer 67 1993 290 296
    • (1993) Br J Cancer , vol.67 , pp. 290-296
    • Pusztai, L.1    Lewis, C.E.2    McGee, J.O.3
  • 31
    • 0033568191 scopus 로고    scopus 로고
    • Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton
    • D.D. Shock, U.P. Naik, J.E. Brittain, S.K. Alahari, J. Sondek, and L.V. Parise Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton Biochem J 342 Pt 3 1999 729 735
    • (1999) Biochem J , vol.342 , Issue.PART 3 , pp. 729-735
    • Shock, D.D.1    Naik, U.P.2    Brittain, J.E.3    Alahari, S.K.4    Sondek, J.5    Parise, L.V.6
  • 32
    • 0033778278 scopus 로고    scopus 로고
    • Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines
    • S. Simizu, and H. Osada Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines Nat Cell Biol 2 2000 852 854
    • (2000) Nat Cell Biol , vol.2 , pp. 852-854
    • Simizu, S.1    Osada, H.2
  • 33
    • 0026665462 scopus 로고
    • Identification of an early-growth-response gene encoding a novel putative protein kinase
    • D.L. Simmons, B.G. Neel, R. Stevens, G. Evett, and R.L. Erikson Identification of an early-growth-response gene encoding a novel putative protein kinase Mol Cell Biol 12 1992 4164 4169
    • (1992) Mol Cell Biol , vol.12 , pp. 4164-4169
    • Simmons, D.L.1    Neel, B.G.2    Stevens, R.3    Evett, G.4    Erikson, R.L.5
  • 34
    • 0036242249 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity
    • Q. Wang, S. Xie, J. Chen, K. Fukasawa, U. Naik, and F. Traganos Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity Mol Cell Biol 22 2002 3450 3459
    • (2002) Mol Cell Biol , vol.22 , pp. 3450-3459
    • Wang, Q.1    Xie, S.2    Chen, J.3    Fukasawa, K.4    Naik, U.5    Traganos, F.6
  • 36
    • 77954956844 scopus 로고    scopus 로고
    • Saunders WS Deficiency in myosin light-chain phosphorylation causes cytokinesis failure and multipolarity in cancer cells
    • Q. Wu, R.M. Sahasrabudhe, L.Z. Luo, D.W. Lewis, and S.M. Gollin Saunders WS Deficiency in myosin light-chain phosphorylation causes cytokinesis failure and multipolarity in cancer cells Oncogene 29 2010 4183 4193
    • (2010) Oncogene , vol.29 , pp. 4183-4193
    • Wu, Q.1    Sahasrabudhe, R.M.2    Luo, L.Z.3    Lewis, D.W.4    Gollin, S.M.5
  • 37
    • 33846904706 scopus 로고    scopus 로고
    • Polo-like kinase 3 is required for entry into S phase
    • W.C. Zimmerman, and R.L. Erikson Polo-like kinase 3 is required for entry into S phase Proc Natl Acad Sci USA 104 2007 1847 1852
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1847-1852
    • Zimmerman, W.C.1    Erikson, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.