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Volumn 6, Issue 9, 2007, Pages 1053-1061

p27Kip1 metabolism: A fascinating labyrinth

Author keywords

Cell division cycle; Cip Kip family; Cyclin dependent kinase; Cyclin dependent kinase inhibitor; p27Kip1

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR 1B;

EID: 34248208651     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.6.9.4142     Document Type: Review
Times cited : (89)

References (122)
  • 1
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: Cyclins revisited
    • Murray AW. Recycling the cell cycle: Cyclins revisited. Cell 2004; 116:221-34.
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.W.1
  • 4
    • 0027731971 scopus 로고
    • Inhibition of CDK2 activity in vivo by an associated 20K regulatory subunit
    • Gu Y, Turck CW, Morgan DO. Inhibition of CDK2 activity in vivo by an associated 20K regulatory subunit. Nature 1993; 366:707-10.
    • (1993) Nature , vol.366 , pp. 707-710
    • Gu, Y.1    Turck, C.W.2    Morgan, D.O.3
  • 6
    • 0028176483 scopus 로고
    • Cloning of p27kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals
    • Polyak K, Lee MH, Erdjument-Bromage H, Koff A, Roberts JM, Tempst P, Massague J. Cloning of p27kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals. Cell 1994; 78:59-66.
    • (1994) Cell , vol.78 , pp. 59-66
    • Polyak, K.1    Lee, M.H.2    Erdjument-Bromage, H.3    Koff, A.4    Roberts, J.M.5    Tempst, P.6    Massague, J.7
  • 7
    • 0028363519 scopus 로고
    • 1 cyclin-cdk protein kinase activity, is related to p21
    • 1 cyclin-cdk protein kinase activity, is related to p21. Cell 1994; 78:67-74.
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 8
    • 0028988158 scopus 로고
    • Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution
    • Lee MH, Reynisdottir I, Massague J. Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution. Genes and Dev 1995; 9:639-49.
    • (1995) Genes and Dev , vol.9 , pp. 639-649
    • Lee, M.H.1    Reynisdottir, I.2    Massague, J.3
  • 10
    • 0028227197 scopus 로고
    • A novel inhibitor of cyclin-Cdk activity detected in TGF-b-arrested epithelial cells
    • Slingerland J, Hengst L, Pan C, Alexander D, Stampfer M, Reed S. A novel inhibitor of cyclin-Cdk activity detected in TGF-b-arrested epithelial cells. Mol Cell Biol 1994; 14:3683-94.
    • (1994) Mol Cell Biol , vol.14 , pp. 3683-3694
    • Slingerland, J.1    Hengst, L.2    Pan, C.3    Alexander, D.4    Stampfer, M.5    Reed, S.6
  • 11
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structures of the p27kip1 cyclin dependent-kinase inhibitor bound to the cyclin A-cdk 2 complex
    • Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP. Crystal structures of the p27kip1 cyclin dependent-kinase inhibitor bound to the cyclin A-cdk 2 complex. Nature 1996; 382:325-31.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 13
    • 0034894258 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27Kip1
    • Flaugh SL, Lumb KJ. Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27Kip1. Biomacromolecules 2001; 2:538-40.
    • (2001) Biomacromolecules , vol.2 , pp. 538-540
    • Flaugh, S.L.1    Lumb, K.J.2
  • 14
    • 0037154116 scopus 로고    scopus 로고
    • Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27Kip1
    • Bienkiewicz EA, Adkins JN, Kevin J, Lumb KJ. Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27Kip1. Biochemistry 2002; 41:752-9.
    • (2002) Biochemistry , vol.41 , pp. 752-759
    • Bienkiewicz, E.A.1    Adkins, J.N.2    Kevin, J.3    Lumb, K.J.4
  • 15
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm. J Mol Biol 1999; 293:321-31.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 17
    • 0029904487 scopus 로고    scopus 로고
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. NACP, a protein implicated in Alzheimer's Disease and learning, is natively unfolded. Biochemistry 1996; 35:13709-15.
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. NACP, a protein implicated in Alzheimer's Disease and learning, is natively unfolded. Biochemistry 1996; 35:13709-15.
  • 18
    • 0034646289 scopus 로고    scopus 로고
    • Campbell KM, Terrell AR, Laybourn PJ, Lumb KJ. Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. Biochemistry 2000; 39:2708-13.
    • Campbell KM, Terrell AR, Laybourn PJ, Lumb KJ. Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. Biochemistry 2000; 39:2708-13.
  • 19
    • 1942466518 scopus 로고    scopus 로고
    • p27kip1 modulates cell migration through the regulation of RhoA activation
    • Besson A, Gurian-West M, Schmidt A, Hall A, Roberts JM. p27kip1 modulates cell migration through the regulation of RhoA activation. Genes and Dev 2004; 18:862-76.
    • (2004) Genes and Dev , vol.18 , pp. 862-876
    • Besson, A.1    Gurian-West, M.2    Schmidt, A.3    Hall, A.4    Roberts, J.M.5
  • 20
    • 0037216528 scopus 로고    scopus 로고
    • Novel p27(kip1) C-terminal scatter domain mediates Rac-dependent cell migration independent of cell cycle arrest functions
    • McAllister SS, Becker-Hapak M, Pintucci G, Pagano M, Dowdy SF. Novel p27(kip1) C-terminal scatter domain mediates Rac-dependent cell migration independent of cell cycle arrest functions. Mol Cell Biol 2003; 23:216-28.
    • (2003) Mol Cell Biol , vol.23 , pp. 216-228
    • McAllister, S.S.1    Becker-Hapak, M.2    Pintucci, G.3    Pagano, M.4    Dowdy, S.F.5
  • 22
    • 0035853813 scopus 로고    scopus 로고
    • Direct binding of the signal-transducing adaptor Grb2 facilitates down-regulation of the Cyclin-dependent Kinase Inhibitor p27Kip1
    • Sugiyama Y, Tomoda K, Tanaka T, Arata Y, Yoneda-Kato N, Kato JY. Direct binding of the signal-transducing adaptor Grb2 facilitates down-regulation of the Cyclin-dependent Kinase Inhibitor p27Kip1. J Biol Chem 2001; 276:12084-90.
    • (2001) J Biol Chem , vol.276 , pp. 12084-12090
    • Sugiyama, Y.1    Tomoda, K.2    Tanaka, T.3    Arata, Y.4    Yoneda-Kato, N.5    Kato, J.Y.6
  • 23
    • 0037570624 scopus 로고    scopus 로고
    • p27Kip1 Inhibition of GRB2-SOS formation can regulate Ras activation
    • Moeller SJ, Head ED, Sheaff RJ. p27Kip1 Inhibition of GRB2-SOS formation can regulate Ras activation. Mol Cell Biol 2003; 23:3735-52.
    • (2003) Mol Cell Biol , vol.23 , pp. 3735-3752
    • Moeller, S.J.1    Head, E.D.2    Sheaff, R.J.3
  • 24
  • 25
    • 0037047268 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation of p27 promotes binding to 14-3-3 and cytoplasmic localization
    • Fujita N, Sato S, Katayama K, Tsuruo T. Akt-dependent phosphorylation of p27 promotes binding to 14-3-3 and cytoplasmic localization. J Biol Chem 2002; 277:28706-13.
    • (2002) J Biol Chem , vol.277 , pp. 28706-28713
    • Fujita, N.1    Sato, S.2    Katayama, K.3    Tsuruo, T.4
  • 26
    • 1542677089 scopus 로고    scopus 로고
    • Phosphorylation of p27 at threonine 198 by p90 ribosomal protein S6 kinase promotes its binding to 14-3-3 and cytoplasmic localization
    • Fujita N, Sato S, Tsuruo T. Phosphorylation of p27 at threonine 198 by p90 ribosomal protein S6 kinase promotes its binding to 14-3-3 and cytoplasmic localization. J Biol Chem 2003; 278:49254-60.
    • (2003) J Biol Chem , vol.278 , pp. 49254-49260
    • Fujita, N.1    Sato, S.2    Tsuruo, T.3
  • 27
    • 3142512358 scopus 로고    scopus 로고
    • 14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27
    • Sekimoto T, Fukumoto M, Yoneda Y. 14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27. EMBO J 2004; 23:1934-42.
    • (2004) EMBO J , vol.23 , pp. 1934-1942
    • Sekimoto, T.1    Fukumoto, M.2    Yoneda, Y.3
  • 28
    • 0033913977 scopus 로고    scopus 로고
    • Minimal requirements for the nuclear localization of p27(Kip1), a cyclin-dependent kinase inhibitor
    • Zeng Y, Hirano K, Hirano M, Nishimura J, Kanaide H. Minimal requirements for the nuclear localization of p27(Kip1), a cyclin-dependent kinase inhibitor. Biochem Biophys Res Commun 2000; 274:37-42.
    • (2000) Biochem Biophys Res Commun , vol.274 , pp. 37-42
    • Zeng, Y.1    Hirano, K.2    Hirano, M.3    Nishimura, J.4    Kanaide, H.5
  • 31
    • 21844431711 scopus 로고    scopus 로고
    • The regulation of S phase initiation by p27Kip1 in NIH3T3 cells
    • Sa G, Guo Y, Stacey DW. The regulation of S phase initiation by p27Kip1 in NIH3T3 cells. Cell Cycle 2005; 4:618-27.
    • (2005) Cell Cycle , vol.4 , pp. 618-627
    • Sa, G.1    Guo, Y.2    Stacey, D.W.3
  • 32
    • 33749591900 scopus 로고    scopus 로고
    • p27Kip1 and cyclin dependent kinase 2 regulate passage through the restriction point
    • Hitomi M, Yang K, Ya, Guo Y, Fretthold J, Harwalkar J, Stacey D. p27Kip1 and cyclin dependent kinase 2 regulate passage through the restriction point. Cell Cycle 2006; 5:2281-9.
    • (2006) Cell Cycle , vol.5 , pp. 2281-2289
    • Hitomi, M.1    Yang, K.2    Ya3    Guo, Y.4    Fretthold, J.5    Harwalkar, J.6    Stacey, D.7
  • 33
    • 25444526687 scopus 로고    scopus 로고
    • Using kinetic studies to uncover new Rb functions in inhibiting cell cycle progression
    • Ji P, Zhu L. Using kinetic studies to uncover new Rb functions in inhibiting cell cycle progression. Cell Cycle 2005; 4:373-5.
    • (2005) Cell Cycle , vol.4 , pp. 373-375
    • Ji, P.1    Zhu, L.2
  • 36
    • 0030010591 scopus 로고    scopus 로고
    • Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors
    • Nakayama K, Ishida N, Shirane M, Inomata A, Inoue T, Shishido N, Horii I, Loh DY, Nakayama K. Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors. Cell 1996; 85:707-20.
    • (1996) Cell , vol.85 , pp. 707-720
    • Nakayama, K.1    Ishida, N.2    Shirane, M.3    Inomata, A.4    Inoue, T.5    Shishido, N.6    Horii, I.7    Loh, D.Y.8    Nakayama, K.9
  • 40
    • 0034092911 scopus 로고    scopus 로고
    • Regulation of the cdk inhibitor p27 and its deregulation in cancer
    • Slingerland J, Pagano M. Regulation of the cdk inhibitor p27 and its deregulation in cancer. J Cell Physiol 2000; 183:10-7.
    • (2000) J Cell Physiol , vol.183 , pp. 10-17
    • Slingerland, J.1    Pagano, M.2
  • 42
    • 0035835828 scopus 로고    scopus 로고
    • p27(Kip1): Regulation and function of a haploinsufficient tumor suppressor and its misregulation in cancer
    • Philipp-Staheli J, Payne S, Kemp C. p27(Kip1): Regulation and function of a haploinsufficient tumor suppressor and its misregulation in cancer. Exp Cell Res 2001; 264:148-68.
    • (2001) Exp Cell Res , vol.264 , pp. 148-168
    • Philipp-Staheli, J.1    Payne, S.2    Kemp, C.3
  • 43
    • 0032511848 scopus 로고    scopus 로고
    • The murine gene p27Kip1 is haplo-insufficient for tumour suppression
    • Fero M, Randel E, Gurley K, Roberts J, Kemp C. The murine gene p27Kip1 is haplo-insufficient for tumour suppression. Nature 1998; 396:177-80.
    • (1998) Nature , vol.396 , pp. 177-180
    • Fero, M.1    Randel, E.2    Gurley, K.3    Roberts, J.4    Kemp, C.5
  • 44
    • 25444504308 scopus 로고    scopus 로고
    • An unusual gene dosage effect of p27Kip1 in a mouse model of prostate cancer
    • Abate-Shen C, Shen MM. An unusual gene dosage effect of p27Kip1 in a mouse model of prostate cancer. Cell Cycle 2005; 4:426-8.
    • (2005) Cell Cycle , vol.4 , pp. 426-428
    • Abate-Shen, C.1    Shen, M.M.2
  • 45
    • 0031439355 scopus 로고    scopus 로고
    • Promoting apoptosis: A novel activity associated with the cyclin-dependent kinase inhibitor p27
    • Katayose Y, Kim M, Rakkar AN, Li Z, Cowan KH, Seth P. Promoting apoptosis: A novel activity associated with the cyclin-dependent kinase inhibitor p27. Cancer Res 1997; 57:5441-5.
    • (1997) Cancer Res , vol.57 , pp. 5441-5445
    • Katayose, Y.1    Kim, M.2    Rakkar, A.N.3    Li, Z.4    Cowan, K.H.5    Seth, P.6
  • 46
    • 0032429122 scopus 로고    scopus 로고
    • Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
    • An B, Goldfarb RH, Siman R, Dou QP. Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell Death Differ 1998; 12:1062-75.
    • (1998) Cell Death Differ , vol.12 , pp. 1062-1075
    • An, B.1    Goldfarb, R.H.2    Siman, R.3    Dou, Q.P.4
  • 47
    • 2342598475 scopus 로고    scopus 로고
    • The role of p27Kip1 in proteasome inhibitor induced apoptosis
    • Drexler HCA. The role of p27Kip1 in proteasome inhibitor induced apoptosis. Cell Cycle 2003; 2:438-41.
    • (2003) Cell Cycle , vol.2 , pp. 438-441
    • Drexler, H.C.A.1
  • 48
    • 0032012062 scopus 로고    scopus 로고
    • Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: Role of a caspase cascade
    • Levkau B, Koyama H, Raines EW, Clurman BE, Herren B, Orth K, Roberts JM, Ross R. Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: Role of a caspase cascade. Mol Cell 1998; 4:553-63.
    • (1998) Mol Cell , vol.4 , pp. 553-563
    • Levkau, B.1    Koyama, H.2    Raines, E.W.3    Clurman, B.E.4    Herren, B.5    Orth, K.6    Roberts, J.M.7    Ross, R.8
  • 49
    • 0033580135 scopus 로고    scopus 로고
    • p27Kip1 induces drug resistance by preventing apoptosis upstream of cytochrome c release and procaspase-3 activation in leukemic cells
    • Eymin B, Haugg M, Droin N, Sordet O, Dimanche-Boitrel MT, Solary E. p27Kip1 induces drug resistance by preventing apoptosis upstream of cytochrome c release and procaspase-3 activation in leukemic cells. Oncogene 1999; 18:1411-8.
    • (1999) Oncogene , vol.18 , pp. 1411-1418
    • Eymin, B.1    Haugg, M.2    Droin, N.3    Sordet, O.4    Dimanche-Boitrel, M.T.5    Solary, E.6
  • 51
    • 0034842489 scopus 로고    scopus 로고
    • Overexpression of p27(Kip1) by doxycycline-regulated adenoviral vectors inhibits endothelial cell proliferation and migration and impairs angiogenesis
    • Goukassian D, Diez-Juan A, Asahara T, Schratzberger P, Silver M, Murayama T, Isner JM, Andres V. Overexpression of p27(Kip1) by doxycycline-regulated adenoviral vectors inhibits endothelial cell proliferation and migration and impairs angiogenesis. FASEB J 2001; 11:1877-85.
    • (2001) FASEB J , vol.11 , pp. 1877-1885
    • Goukassian, D.1    Diez-Juan, A.2    Asahara, T.3    Schratzberger, P.4    Silver, M.5    Murayama, T.6    Isner, J.M.7    Andres, V.8
  • 53
    • 0037423864 scopus 로고    scopus 로고
    • Coordinate control of proliferation and migration by the p27 Kip1/cyclin-dependent kinase/Retinoblastoma pathway in vascular smooth muscle cells and fibroblasts
    • Diez-Juan A, Andres V. Coordinate control of proliferation and migration by the p27 Kip1/cyclin-dependent kinase/Retinoblastoma pathway in vascular smooth muscle cells and fibroblasts. Circ Res 2003; 92:402-10.
    • (2003) Circ Res , vol.92 , pp. 402-410
    • Diez-Juan, A.1    Andres, V.2
  • 54
    • 0642375769 scopus 로고    scopus 로고
    • Effect of p27 Kip1 on the ability of invasion and metastasis of an oral cancer cell line
    • Supriatno, Harada K, Kawaguchi S, Yoshida H, Sato M. Effect of p27 Kip1 on the ability of invasion and metastasis of an oral cancer cell line. Oncol Rep 2003; 10:527-32.
    • (2003) Oncol Rep , vol.10 , pp. 527-532
    • Supriatno1    Harada, K.2    Kawaguchi, S.3    Yoshida, H.4    Sato, M.5
  • 55
    • 33751255370 scopus 로고    scopus 로고
    • Coupling cell cycle exit, neuronal differentiation and migration in cortical neurogenesis
    • Nguyen L, Besson A, Roberts JM, Guillemot F. Coupling cell cycle exit, neuronal differentiation and migration in cortical neurogenesis. Cell Cycle 2006; 5:2314-8.
    • (2006) Cell Cycle , vol.5 , pp. 2314-2318
    • Nguyen, L.1    Besson, A.2    Roberts, J.M.3    Guillemot, F.4
  • 56
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion,and adhesion during cell movement
    • Nobes C, Hall A. Rho GTPases control polarity, protrusion,and adhesion during cell movement. J Cell Biol 1999; 144:1235-44.
    • (1999) J Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.1    Hall, A.2
  • 57
    • 0035833247 scopus 로고    scopus 로고
    • RhoA is required for monocyte tail retraction durino transendothelial migration
    • Worthylake R, Lemoine S, Watson J, Burridge K. RhoA is required for monocyte tail retraction durino transendothelial migration. J Cell Biol 2001; 154:147-60.
    • (2001) J Cell Biol , vol.154 , pp. 147-160
    • Worthylake, R.1    Lemoine, S.2    Watson, J.3    Burridge, K.4
  • 59
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • Arthur WT, Burridge K. RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol Biol Cell 2001; 12:2711-20.
    • (2001) Mol Biol Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 60
    • 0035152391 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases
    • Cox EA, Sastry SK, Huttenlocher A. Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases. Mol Biol Cell 2001; 12:265-77.
    • (2001) Mol Biol Cell , vol.12 , pp. 265-277
    • Cox, E.A.1    Sastry, S.K.2    Huttenlocher, A.3
  • 61
    • 0035865137 scopus 로고    scopus 로고
    • Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility
    • Sahai E, Olson MF, Marshall CJ. Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility. EMBO J 2001; 20:755-66.
    • (2001) EMBO J , vol.20 , pp. 755-766
    • Sahai, E.1    Olson, M.F.2    Marshall, C.J.3
  • 62
    • 0042349229 scopus 로고    scopus 로고
    • ERK-MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility
    • Vial E, Sahai E, Marshall CJ. ERK-MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility. Cancer Cell 2003; 4:67-79.
    • (2003) Cancer Cell , vol.4 , pp. 67-79
    • Vial, E.1    Sahai, E.2    Marshall, C.J.3
  • 63
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992; 70:389-99.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 65
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature 2002; 420:629-35.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 66
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly,disassembly and turnover in migrating cells - Over and over and over again
    • Webb DJ, Parsons JT, Horwitz AF. Adhesion assembly,disassembly and turnover in migrating cells - Over and over and over again. Nat Cell Biol 2002; 4:E97-100.
    • (2002) Nat Cell Biol , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 67
    • 0037157872 scopus 로고    scopus 로고
    • Cytoplasmic p21 Cip1/Waf1 regulates neurite remodeling by inhibiting Rho-kinase activity
    • Tanaka H, Yamashita T, Asada M, Mizutani S, Yoshikawa H, Tohyama M. Cytoplasmic p21 Cip1/Waf1 regulates neurite remodeling by inhibiting Rho-kinase activity. J Cell Biol 2002; 158:321-9.
    • (2002) J Cell Biol , vol.158 , pp. 321-329
    • Tanaka, H.1    Yamashita, T.2    Asada, M.3    Mizutani, S.4    Yoshikawa, H.5    Tohyama, M.6
  • 68
    • 0347717882 scopus 로고    scopus 로고
    • Cytoplasmic p21 is involved in Ras-induced inhibition of the ROCK/LIMK/Cofilin pathway
    • Lee S, Helfman DM. Cytoplasmic p21 is involved in Ras-induced inhibition of the ROCK/LIMK/Cofilin pathway. J Biol Chem 2003; 279:1885-91.
    • (2003) J Biol Chem , vol.279 , pp. 1885-1891
    • Lee, S.1    Helfman, D.M.2
  • 71
    • 0032537819 scopus 로고    scopus 로고
    • Signals from Ras and Rho GTPases interact to regulate expression of p21 Waf1/Cip1
    • Olson MF, Paterson HF, Marshall CJ. Signals from Ras and Rho GTPases interact to regulate expression of p21 Waf1/Cip1. Nature 1998; 394:295-9.
    • (1998) Nature , vol.394 , pp. 295-299
    • Olson, M.F.1    Paterson, H.F.2    Marshall, C.J.3
  • 72
    • 0033525188 scopus 로고    scopus 로고
    • RhoA stimulates p27 Kip1 degradation through its regulation of cyclin E/CDK2 activity
    • Hu W, Bellone C, Baldassare J. RhoA stimulates p27 Kip1 degradation through its regulation of cyclin E/CDK2 activity. J Biol Chem 1999; 274:3396-401.
    • (1999) J Biol Chem , vol.274 , pp. 3396-3401
    • Hu, W.1    Bellone, C.2    Baldassare, J.3
  • 73
    • 0037053407 scopus 로고    scopus 로고
    • Rho activity can alter the translation of mRNA and is important for Ras V12 -induced transformation in a manner dependent on p27 status
    • Vidal A, Millard S, Miller J, Koff A. Rho activity can alter the translation of mRNA and is important for Ras V12 -induced transformation in a manner dependent on p27 status. J Biol Chem 2002; 277:16433-40.
    • (2002) J Biol Chem , vol.277 , pp. 16433-16440
    • Vidal, A.1    Millard, S.2    Miller, J.3    Koff, A.4
  • 74
    • 0347717882 scopus 로고    scopus 로고
    • Cytoplasmic p21Cip1 is involved in Ras-induced inhibition of the ROCK/LIMK/cofilin pathway
    • Lee S, Helfman DM. Cytoplasmic p21Cip1 is involved in Ras-induced inhibition of the ROCK/LIMK/cofilin pathway. J Biol Chem 2004; 279:1885-91.
    • (2004) J Biol Chem , vol.279 , pp. 1885-1891
    • Lee, S.1    Helfman, D.M.2
  • 75
    • 0034643331 scopus 로고    scopus 로고
    • AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
    • Medema RH, Kops GJ, Bos JL, Burgering BM. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. Nature 2000; 404:782-7.
    • (2000) Nature , vol.404 , pp. 782-787
    • Medema, R.H.1    Kops, G.J.2    Bos, J.L.3    Burgering, B.M.4
  • 79
    • 0037094096 scopus 로고    scopus 로고
    • The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2
    • Stahl M, Dijkers PF, Kops GJ, Lens SM, Coffer PJ, Burgering BM, Medema RH. The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2. J Immunol 2002; 168:5024-31.
    • (2002) J Immunol , vol.168 , pp. 5024-5031
    • Stahl, M.1    Dijkers, P.F.2    Kops, G.J.3    Lens, S.M.4    Coffer, P.J.5    Burgering, B.M.6    Medema, R.H.7
  • 80
    • 0037113939 scopus 로고    scopus 로고
    • Increased hepatic forkhead box M1B (FoxM1B) levels in old-aged mice stimulated liver regeneration through diminished p27Kip1 protein levels and increased Cdc25B expression
    • Wang X, Krupczak-Hollis K, Tan Y, Dennewitz MB, Adami GR, Costa RH. Increased hepatic forkhead box M1B (FoxM1B) levels in old-aged mice stimulated liver regeneration through diminished p27Kip1 protein levels and increased Cdc25B expression. J Biol Chem 2002; 277:44310-6.
    • (2002) J Biol Chem , vol.277 , pp. 44310-44316
    • Wang, X.1    Krupczak-Hollis, K.2    Tan, Y.3    Dennewitz, M.B.4    Adami, G.R.5    Costa, R.H.6
  • 81
    • 0037017396 scopus 로고    scopus 로고
    • Dijkers PF, Birkenkamp KU, Lam EWF, N Thomas SB, Lammers JWJ, Koenderman L, Coffer PJ. FKHR-L1 can act as a critical effector of cell death induced by cytokine withdrawal: Protein kinase B-enhanced cell survival through maintenance of mitochondrial integrity. J Cell Biol 2002; 156:531-42.
    • Dijkers PF, Birkenkamp KU, Lam EWF, N Thomas SB, Lammers JWJ, Koenderman L, Coffer PJ. FKHR-L1 can act as a critical effector of cell death induced by cytokine withdrawal: Protein kinase B-enhanced cell survival through maintenance of mitochondrial integrity. J Cell Biol 2002; 156:531-42.
  • 83
    • 2142662252 scopus 로고    scopus 로고
    • Reciprocal control of forkhead box O3a and c-myc via the phosphatidylinositol 3-kinase pathway coordinately regulates p27Kip1 levels
    • Chandramohan V, Jeay S, Pianetti S, Sonenshein SGE. Reciprocal control of forkhead box O3a and c-myc via the phosphatidylinositol 3-kinase pathway coordinately regulates p27Kip1 levels. J Immunol 2004; 172:5522-7.
    • (2004) J Immunol , vol.172 , pp. 5522-5527
    • Chandramohan, V.1    Jeay, S.2    Pianetti, S.3    Sonenshein, S.G.E.4
  • 85
    • 0035093090 scopus 로고    scopus 로고
    • Role of Sp1 in the induction of p27 gene expression in vascular smooth muscle cells in vitro and after balloon angioplasty
    • Andrés V, Ureña J, Poch E, Chen D, Goukassian D. Role of Sp1 in the induction of p27 gene expression in vascular smooth muscle cells in vitro and after balloon angioplasty. Arteriosclerosis Thrombosis and Vascular Biology 2001; 21:342-7.
    • (2001) Arteriosclerosis Thrombosis and Vascular Biology , vol.21 , pp. 342-347
    • Andrés, V.1    Ureña, J.2    Poch, E.3    Chen, D.4    Goukassian, D.5
  • 88
    • 0036799377 scopus 로고    scopus 로고
    • PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization
    • Shin I, Yakes FM, Rojo F, Shin NY, Bakin AV, Baselga J, Arteaga CL. PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization. Nat Med 2002; 8:1145-52.
    • (2002) Nat Med , vol.8 , pp. 1145-1152
    • Shin, I.1    Yakes, F.M.2    Rojo, F.3    Shin, N.Y.4    Bakin, A.V.5    Baselga, J.6    Arteaga, C.L.7
  • 90
    • 0037047268 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization
    • Fujita N, Sato S, Katayama K, Tsuruo T. Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. J Biol Chem 2002; 277:28706-13.
    • (2002) J Biol Chem , vol.277 , pp. 28706-28713
    • Fujita, N.1    Sato, S.2    Katayama, K.3    Tsuruo, T.4
  • 91
    • 1542677089 scopus 로고    scopus 로고
    • Phosphorylation of p27Kip1 at threonine 198 by p90 localization
    • Fujita N, Sato S, Tsuruo T. Phosphorylation of p27Kip1 at threonine 198 by p90 localization. J Biol Chem 2003; 278:49254-60.
    • (2003) J Biol Chem , vol.278 , pp. 49254-49260
    • Fujita, N.1    Sato, S.2    Tsuruo, T.3
  • 92
    • 0042197268 scopus 로고    scopus 로고
    • Focus on p27. Are p27 and p21 cytoplasmic oncoproteins?
    • Blagosklonny MV. Focus on p27. Are p27 and p21 cytoplasmic oncoproteins? Cell Cycle 2002; 1:391-3.
    • (2002) Cell Cycle , vol.1 , pp. 391-393
    • Blagosklonny, M.V.1
  • 93
    • 0041696635 scopus 로고    scopus 로고
    • Focus on p27: Keeping p27 Kip1 in the cytoplasm: A second front in cancer's war on p27
    • Reed SI. Focus on p27: Keeping p27 Kip1 in the cytoplasm: A second front in cancer's war on p27. Cell Cycle 2002; 1:389-90.
    • (2002) Cell Cycle , vol.1 , pp. 389-390
    • Reed, S.I.1
  • 94
    • 3142512358 scopus 로고    scopus 로고
    • 14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27(Kip1)
    • Sekimoto T, Fukumoto M, Yoneda Y. 14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27(Kip1). EMBO J 2004; 23:1934-42.
    • (2004) EMBO J , vol.23 , pp. 1934-1942
    • Sekimoto, T.1    Fukumoto, M.2    Yoneda, Y.3
  • 95
    • 31544471421 scopus 로고    scopus 로고
    • Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27 Kip1 in the acute promyelocytic leukemia cell line NB4
    • Kardinal C, Dangers M, Kardinal A, Koch A, Brandt DT, Tamura T, Welte K. Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27 Kip1 in the acute promyelocytic leukemia cell line NB4. Blood 2006; 107:1133-40.
    • (2006) Blood , vol.107 , pp. 1133-1140
    • Kardinal, C.1    Dangers, M.2    Kardinal, A.3    Koch, A.4    Brandt, D.T.5    Tamura, T.6    Welte, K.7
  • 96
    • 0037177386 scopus 로고    scopus 로고
    • Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export
    • Ishida N, Hara T, Kamura T, Yoshida M, Nakayama K, Nakayama KI. Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export. J Biol Chem 2002; 277:14355-8.
    • (2002) J Biol Chem , vol.277 , pp. 14355-14358
    • Ishida, N.1    Hara, T.2    Kamura, T.3    Yoshida, M.4    Nakayama, K.5    Nakayama, K.I.6
  • 97
    • 0033545636 scopus 로고    scopus 로고
    • Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1
    • Tomoda K, Kubota Y, Kato J. Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1. Nature 1999; 398:160-5.
    • (1999) Nature , vol.398 , pp. 160-165
    • Tomoda, K.1    Kubota, Y.2    Kato, J.3
  • 98
    • 0034682818 scopus 로고    scopus 로고
    • Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability
    • Ishida N, Kitagawa M, Hatakeyama S, Nakayama K. Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability. J Biol Chem 2000; 275:25146-54.
    • (2000) J Biol Chem , vol.275 , pp. 25146-25154
    • Ishida, N.1    Kitagawa, M.2    Hatakeyama, S.3    Nakayama, K.4
  • 99
    • 12544259437 scopus 로고    scopus 로고
    • Role of serine 10 phosphorylation in p27 stabilization revealed by analysis of p27 knock-in mice harboring a serine 10 mutation
    • Kotake Y, Nakayama K, Ishida N, Nakayama KI. Role of serine 10 phosphorylation in p27 stabilization revealed by analysis of p27 knock-in mice harboring a serine 10 mutation. J Biol Chem 2005; 280:1095-102.
    • (2005) J Biol Chem , vol.280 , pp. 1095-1102
    • Kotake, Y.1    Nakayama, K.2    Ishida, N.3    Nakayama, K.I.4
  • 100
  • 101
    • 0030997297 scopus 로고    scopus 로고
    • Regulation of the cyclin-dependent kinase inhibitor p27 by degradation and phosphorylation
    • Alessandrini A, Chiaur DS, Pagano M. Regulation of the cyclin-dependent kinase inhibitor p27 by degradation and phosphorylation. Leukemia 1997; 11:342-5.
    • (1997) Leukemia , vol.11 , pp. 342-345
    • Alessandrini, A.1    Chiaur, D.S.2    Pagano, M.3
  • 102
    • 0036645678 scopus 로고    scopus 로고
    • A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression
    • Boehm M, Yoshimoto T, Crook MF, Nallamshetty S, True A, Nabel GJ, Nabel EG. A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression. EMBO J 2002; 21:3390-401.
    • (2002) EMBO J , vol.21 , pp. 3390-3401
    • Boehm, M.1    Yoshimoto, T.2    Crook, M.F.3    Nallamshetty, S.4    True, A.5    Nabel, G.J.6    Nabel, E.G.7
  • 103
    • 2542489078 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor p27Kip1 is stabilized in G0 by Mirk/dyrk1B kinase
    • Deng X, Mercer SE, Shah S, Ewton DZ, Friedman E. The cyclin-dependent kinase inhibitor p27Kip1 is stabilized in G0 by Mirk/dyrk1B kinase. J Biol Chem 2004; 279:22498-504.
    • (2004) J Biol Chem , vol.279 , pp. 22498-22504
    • Deng, X.1    Mercer, S.E.2    Shah, S.3    Ewton, D.Z.4    Friedman, E.5
  • 104
    • 34248401210 scopus 로고    scopus 로고
    • Akt1 sequentially phosphorylates p27kip1 within a conserved but noncanonical region
    • Nacusi LP, Sheaff RJ. Akt1 sequentially phosphorylates p27kip1 within a conserved but noncanonical region. Cell Division 2006; 1:11-38.
    • (2006) Cell Division , vol.1 , pp. 11-38
    • Nacusi, L.P.1    Sheaff, R.J.2
  • 106
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27
    • Vlach J, Hennecke S, Amati B. Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27. EMBO J 1997; 16:5334-44.
    • (1997) EMBO J , vol.16 , pp. 5334-5344
    • Vlach, J.1    Hennecke, S.2    Amati, B.3
  • 107
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano AC, Eytan E, Hershko A, Pagano M. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1999; 1:193-9.
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 109
    • 0033578073 scopus 로고    scopus 로고
    • p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov LM, Yeh KH, Lee SJ, Sun H, Zhang H. p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr Biol 1999; 9:661-4.
    • (1999) Curr Biol , vol.9 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 114
    • 0042378825 scopus 로고    scopus 로고
    • Erk 1,2 phosphorylates p27Kip1: Functional evidence for a role in high glucose-induced hypertrophy of mesangial cells
    • Wolf G, Reinking R, Zahner G, Stahl RAK, Shankland SJ. Erk 1,2 phosphorylates p27Kip1: Functional evidence for a role in high glucose-induced hypertrophy of mesangial cells. Diabetologia 2003; 46:1090-9.
    • (2003) Diabetologia , vol.46 , pp. 1090-1099
    • Wolf, G.1    Reinking, R.2    Zahner, G.3    Stahl, R.A.K.4    Shankland, S.J.5
  • 117
    • 0032757489 scopus 로고    scopus 로고
    • Structure and expression of the gene encoding mouse F-box protein, Fwd2
    • Miura M, Hatakeyama S, Hattori K, Nakayama K. Structure and expression of the gene encoding mouse F-box protein, Fwd2. Genomics 1999; 62:50-8.
    • (1999) Genomics , vol.62 , pp. 50-58
    • Miura, M.1    Hatakeyama, S.2    Hattori, K.3    Nakayama, K.4
  • 119
    • 24044555556 scopus 로고    scopus 로고
    • Molecular dissection of the interaction between p27 and Kip1 ubiquitylation-promoting complex, the ubiquitin ligase that regulates proteolysis of p27 in G1 phase
    • Kotoshiba S, Kamura T, Hara T, Ishida N, Nakayama KI. Molecular dissection of the interaction between p27 and Kip1 ubiquitylation-promoting complex, the ubiquitin ligase that regulates proteolysis of p27 in G1 phase. J Biol Chem 2005; 280:17694-700.
    • (2005) J Biol Chem , vol.280 , pp. 17694-17700
    • Kotoshiba, S.1    Kamura, T.2    Hara, T.3    Ishida, N.4    Nakayama, K.I.5
  • 121
    • 0034625418 scopus 로고    scopus 로고
    • Mitotic clonal expansion during preadipocyte differentiation: Calpain-mediated sturnover of p27
    • Patel YM, Lane MD. Mitotic clonal expansion during preadipocyte differentiation: Calpain-mediated sturnover of p27. J Biol Chem 2000; 275:17653-60.
    • (2000) J Biol Chem , vol.275 , pp. 17653-17660
    • Patel, Y.M.1    Lane, M.D.2
  • 122
    • 0038485631 scopus 로고    scopus 로고
    • MAP kinase-dependent degradation of p27Kip1 by calpains in choroidal melanoma cells: Requirement of p27Kip1 nuclear export
    • Delmas C, Aragou N, Poussard S, Cottin P, Darbon JM, Manenti S. MAP kinase-dependent degradation of p27Kip1 by calpains in choroidal melanoma cells: Requirement of p27Kip1 nuclear export. J Biol Chem 2003; 278:12443-51.
    • (2003) J Biol Chem , vol.278 , pp. 12443-12451
    • Delmas, C.1    Aragou, N.2    Poussard, S.3    Cottin, P.4    Darbon, J.M.5    Manenti, S.6


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