메뉴 건너뛰기




Volumn 32, Issue 11, 2012, Pages 2083-2098

Hydrophobic motif phosphorylation coordinates activity and polar localization of the neurospora crassa nuclear Dbf2-related kinase COT1

Author keywords

[No Author keywords available]

Indexed keywords

COT1 PROTEIN; FUNGAL PROTEIN; MOB2 PROTEIN; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 84864022675     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.06263-11     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 80555148801 scopus 로고    scopus 로고
    • Functional characterization and cellular dynamics of the CDC-42-RAC-CDC-24 module in Neurospora crassa
    • Araujo-Palomares CL, Richthammer C, Seiler S, Castro-Longoria E. 2011. Functional characterization and cellular dynamics of the CDC-42-RAC-CDC-24 module in Neurospora crassa. PLoS One 6:e27148.
    • (2011) PLoS One , vol.6
    • Araujo-Palomares, C.L.1    Richthammer, C.2    Seiler, S.3    Castro-Longoria, E.4
  • 2
    • 71649113079 scopus 로고    scopus 로고
    • Roles of mammalian sterile 20-like kinase 2-dependent phosphorylations of Mps one binder 1B in the activation of nuclear Dbf2-related kinases
    • Bao Y, et al. 2009. Roles of mammalian sterile 20-like kinase 2-dependent phosphorylations of Mps one binder 1B in the activation of nuclear Dbf2-related kinases. Genes Cells 14:1369-1381.
    • (2009) Genes Cells , vol.14 , pp. 1369-1381
    • Bao, Y.1
  • 3
    • 40849086680 scopus 로고    scopus 로고
    • Characterization of interactions between and among components of the meiotic silencing by unpaired DNA machinery in Neurospora crassa using bimolecular fluorescence complementation
    • Bardiya N, et al. 2008. Characterization of interactions between and among components of the meiotic silencing by unpaired DNA machinery in Neurospora crassa using bimolecular fluorescence complementation. Genetics 178:593-596.
    • (2008) Genetics , vol.178 , pp. 593-596
    • Bardiya, N.1
  • 4
    • 0033565608 scopus 로고    scopus 로고
    • The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
    • Behn-Krappa A, Newton AC. 1999. The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation. Curr. Biol. 9:728-737.
    • (1999) Curr. Biol. , vol.9 , pp. 728-737
    • Behn-Krappa, A.1    Newton, A.C.2
  • 5
    • 4143117852 scopus 로고    scopus 로고
    • Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein
    • Bichsel SJ, Tamaskovic R, Stegert MR, Hemmings BA. 2004. Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein. J. Biol. Chem. 279:35228-35235.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35228-35235
    • Bichsel, S.J.1    Tamaskovic, R.2    Stegert, M.R.3    Hemmings, B.A.4
  • 6
    • 0034161251 scopus 로고    scopus 로고
    • Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    • Biondi RM, et al. 2000. Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA. EMBO J. 19:979-988.
    • (2000) EMBO J , vol.19 , pp. 979-988
    • Biondi, R.M.1
  • 7
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi RM, Nebreda AR. 2003. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372:1-13.
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 8
    • 79251540864 scopus 로고    scopus 로고
    • Mitotic exit control of the Saccharomyces cerevisiae Ndr/LATS kinase Cbk1 regulates daughter cell separation after cytokinesis
    • Brace J, Hsu J, Weiss EL. 2011. Mitotic exit control of the Saccharomyces cerevisiae Ndr/LATS kinase Cbk1 regulates daughter cell separation after cytokinesis. Mol. Cell. Biol. 31:721-735.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 721-735
    • Brace, J.1    Hsu, J.2    Weiss, E.L.3
  • 9
    • 16444373346 scopus 로고    scopus 로고
    • The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1
    • Chan EH, et al. 2005. The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1. Oncogene 24:2076-2086.
    • (2005) Oncogene , vol.24 , pp. 2076-2086
    • Chan, E.H.1
  • 10
    • 0035341895 scopus 로고    scopus 로고
    • The Ste20 group kinases as regulators of MAP kinase cascades
    • Dan I, Watanabe NM, Kusumi A. 2001. The Ste20 group kinases as regulators of MAP kinase cascades. Trends Cell Biol. 11:220-230.
    • (2001) Trends Cell Biol , vol.11 , pp. 220-230
    • Dan, I.1    Watanabe, N.M.2    Kusumi, A.3
  • 11
    • 5144222766 scopus 로고    scopus 로고
    • Control of dendritic branching and tiling by the Tricornered-kinase/Furry signaling pathway in Drosophila sensory neurons
    • Emoto K, et al. 2004. Control of dendritic branching and tiling by the Tricornered-kinase/Furry signaling pathway in Drosophila sensory neurons. Cell 119:245-256.
    • (2004) Cell , vol.119 , pp. 245-256
    • Emoto, K.1
  • 12
    • 33748664773 scopus 로고    scopus 로고
    • The tumour suppressor Hippo acts with the NDR kinases in dendritic tiling and maintenance
    • Emoto K, Parrish JZ, Jan LY, Jan YN. 2006. The tumour suppressor Hippo acts with the NDR kinases in dendritic tiling and maintenance. Nature 443:210-213.
    • (2006) Nature , vol.443 , pp. 210-213
    • Emoto, K.1    Parrish, J.Z.2    Jan, L.Y.3    Jan, Y.N.4
  • 13
    • 33751583820 scopus 로고    scopus 로고
    • Allosteric activation of the protein kinase PDK1 with low molecular weight compounds
    • Engel M, et al. 2006. Allosteric activation of the protein kinase PDK1 with low molecular weight compounds. EMBO J. 25:5469-5480.
    • (2006) EMBO J , vol.25 , pp. 5469-5480
    • Engel, M.1
  • 14
    • 77952308961 scopus 로고    scopus 로고
    • Regulation of cell shape, wing hair initiation and the actin cytoskeleton by Trc/Fry and Wts/Mats complexes
    • Fang X, Adler PN. 2010. Regulation of cell shape, wing hair initiation and the actin cytoskeleton by Trc/Fry and Wts/Mats complexes. Dev. Biol. 341:360-374.
    • (2010) Dev. Biol. , vol.341 , pp. 360-374
    • Fang, X.1    Adler, P.N.2
  • 15
    • 4444362481 scopus 로고    scopus 로고
    • GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa
    • Freitag M, Hickey PC, Raju NB, Selker EU, Read ND. 2004. GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa. Fungal Genet. Biol. 41:897-910.
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 897-910
    • Freitag, M.1    Hickey, P.C.2    Raju, N.B.3    Selker, E.U.4    Read, N.D.5
  • 16
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • Frodin M, et al. 2002. A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation. EMBO J. 21:5396-5407.
    • (2002) EMBO J , vol.21 , pp. 5396-5407
    • Frodin, M.1
  • 17
    • 5144222592 scopus 로고    scopus 로고
    • Mechanosensory neurite termination and tiling depend on SAX-2 and the SAX-1 kinase
    • Gallegos ME, Bargmann CI. 2004. Mechanosensory neurite termination and tiling depend on SAX-2 and the SAX-1 kinase. Neuron 44:239-249.
    • (2004) Neuron , vol.44 , pp. 239-249
    • Gallegos, M.E.1    Bargmann, C.I.2
  • 18
    • 0035380478 scopus 로고    scopus 로고
    • The carboxyl terminus of protein kinase C provides a switch to regulate its interaction with the phosphoinositide-dependent kinase
    • Gao T, Toker A, Newton AC. 2001. The carboxyl terminus of protein kinase C provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, PDK-1. J. Biol. Chem. 276:19588-19596.
    • (2001) PDK-1. J. Biol. Chem. , vol.276 , pp. 19588-19596
    • Gao, T.1    Toker, A.2    Newton, A.C.3
  • 19
    • 0034535198 scopus 로고    scopus 로고
    • The tricornered gene, which is required for the integrity of epidermal cell extensions, encodes the Drosophila nuclear DBF2-related kinase
    • Geng W, He B, Wang M, Adler PN. 2000. The tricornered gene, which is required for the integrity of epidermal cell extensions, encodes the Drosophila nuclear DBF2-related kinase. Genetics 156:1817-1828.
    • (2000) Genetics , vol.156 , pp. 1817-1828
    • Geng, W.1    He, B.2    Wang, M.3    Adler, P.N.4
  • 20
    • 13844322292 scopus 로고    scopus 로고
    • Polarisome meets Spitzenkorper, microscopy, genetics, and genomics converge
    • Harris SD, et al. 2005. Polarisome meets Spitzenkorper: microscopy, genetics, and genomics converge. Eukaryot. Cell 4:225-229.
    • (2005) Eukaryot. Cell , vol.4 , pp. 225-229
    • Harris, S.D.1
  • 21
    • 24344463858 scopus 로고    scopus 로고
    • Drosophila Mob family proteins interact with the related tricornered (Trc) and warts (Wts) kinases
    • He Y, et al. 2005. Drosophila Mob family proteins interact with the related tricornered (Trc) and warts (Wts) kinases. Mol. Biol. Cell 16:4139-4152.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4139-4152
    • He, Y.1
  • 22
    • 12844272737 scopus 로고    scopus 로고
    • The tricornered Ser/Thr protein kinase is regulated by phosphorylation and interacts with furry during Drosophila wing hair development
    • He Y, Fang X, Emoto K, Jan YN, Adler PN. 2005. The tricornered Ser/Thr protein kinase is regulated by phosphorylation and interacts with furry during Drosophila wing hair development. Mol. Biol. Cell 16:689-700.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 689-700
    • He, Y.1    Fang, X.2    Emoto, K.3    Jan, Y.N.4    Adler, P.N.5
  • 23
    • 24344474135 scopus 로고    scopus 로고
    • Human NDR kinases are rapidly activated by MOB proteins through recruitment to the plasma membrane and phosphorylation
    • Hergovich A, Bichsel SJ, Hemmings BA. 2005. Human NDR kinases are rapidly activated by MOB proteins through recruitment to the plasma membrane and phosphorylation. Mol. Cell. Biol. 25:8259-8272.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8259-8272
    • Hergovich, A.1    Bichsel, S.J.2    Hemmings, B.A.3
  • 24
    • 70449723123 scopus 로고    scopus 로고
    • Mammalian NDR/LATS protein kinases in hippo tumor suppressor signaling
    • Hergovich A, Hemmings BA. 2009. Mammalian NDR/LATS protein kinases in hippo tumor suppressor signaling. Biofactors 35:338-345.
    • (2009) Biofactors , vol.35 , pp. 338-345
    • Hergovich, A.1    Hemmings, B.A.2
  • 26
    • 47549115586 scopus 로고    scopus 로고
    • Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1
    • Hirabayashi S, et al. 2008. Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1. Oncogene 27:4281-4292.
    • (2008) Oncogene , vol.27 , pp. 4281-4292
    • Hirabayashi, S.1
  • 27
    • 72649099866 scopus 로고    scopus 로고
    • Mob as tumor suppressor is activated at the cell membrane to control tissue growth and organ size in Drosophila
    • Ho LL, Wei X, Shimizu T, Lai ZC. 2010. Mob as tumor suppressor is activated at the cell membrane to control tissue growth and organ size in Drosophila. Dev. Biol. 337:274-283.
    • (2010) Dev. Biol. , vol.337 , pp. 274-283
    • Ho, L.L.1    Wei, X.2    Shimizu, T.3    Lai, Z.C.4
  • 28
    • 1842557650 scopus 로고    scopus 로고
    • Initiation of cytokinesis is controlled through multiple modes of regulation of the Sid2p-Mob1p kinase complex
    • Hou MC, Guertin DA, McCollum D. 2004. Initiation of cytokinesis is controlled through multiple modes of regulation of the Sid2p-Mob1p kinase complex. Mol. Cell. Biol. 24:3262-3276.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3262-3276
    • Hou, M.C.1    Guertin, D.A.2    McCollum, D.3
  • 29
    • 0037428455 scopus 로고    scopus 로고
    • Nak1, an essential germinal center (GC) kinase regulates cell morphology and growth in Schizosaccharomyces pombe
    • Huang TY, Markley NA, Young D. 2003. Nak1, an essential germinal center (GC) kinase regulates cell morphology and growth in Schizosaccharomyces pombe. J. Biol. Chem. 278:991-997.
    • (2003) J. Biol. Chem. , vol.278 , pp. 991-997
    • Huang, T.Y.1    Markley, N.A.2    Young, D.3
  • 30
    • 33845324116 scopus 로고    scopus 로고
    • Phosphoregulation of Cbk1 is critical for RAM network control of transcription and morphogenesis
    • Jansen JM, Barry MF, Yoo CK, Weiss EL. 2006. Phosphoregulation of Cbk1 is critical for RAM network control of transcription and morphogenesis. J. Cell Biol. 175:755-766.
    • (2006) J. Cell Biol. , vol.175 , pp. 755-766
    • Jansen, J.M.1    Barry, M.F.2    Yoo, C.K.3    Weiss, E.L.4
  • 31
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases, structural basis for regulation
    • Johnson LN, Noble ME, Owen DJ. 1996. Active and inactive protein kinases: structural basis for regulation. Cell 85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 32
    • 77950243325 scopus 로고    scopus 로고
    • Septum formation is regulated by the RHO4-specific exchange factors BUD3 and RGF3 and by the landmark protein BUD4 in Neurospora crassa
    • Justa-Schuch D, Heilig Y, Richthammer C, Seiler S. 2010. Septum formation is regulated by the RHO4-specific exchange factors BUD3 and RGF3 and by the landmark protein BUD4 in Neurospora crassa. Mol. Microbiol. 76:220-235.
    • (2010) Mol. Microbiol. , vol.76 , pp. 220-235
    • Justa-Schuch, D.1    Heilig, Y.2    Richthammer, C.3    Seiler, S.4
  • 33
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen LM, Dutil EM, Newton AC. 1995. Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr. Biol. 5:1394-1403.
    • (1995) Curr. Biol. , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 34
    • 45549084379 scopus 로고    scopus 로고
    • Kinetic mechanism of fully activated S6K1 protein kinase
    • Keshwani MM, Harris TK. 2008. Kinetic mechanism of fully activated S6K1 protein kinase. J. Biol. Chem. 283:11972-11980.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11972-11980
    • Keshwani, M.M.1    Harris, T.K.2
  • 35
    • 77956701458 scopus 로고    scopus 로고
    • Differential NDR/LATS interactions with the humanMOBfamily reveal a negative role for human MOB2 in the regulation of human NDR kinases
    • Kohler RS, Schmitz D, Cornils H, Hemmings BA, Hergovich A. 2010. Differential NDR/LATS interactions with the humanMOBfamily reveal a negative role for human MOB2 in the regulation of human NDR kinases. Mol. Cell. Biol. 30:4507-4520.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4507-4520
    • Kohler, R.S.1    Schmitz, D.2    Cornils, H.3    Hemmings, B.A.4    Hergovich, A.5
  • 36
    • 14844297327 scopus 로고    scopus 로고
    • Control of cell proliferation and apoptosis by mob as tumor suppressor, mats
    • Lai ZC, et al. 2005. Control of cell proliferation and apoptosis by mob as tumor suppressor, mats. Cell 120:675-685.
    • (2005) Cell , vol.120 , pp. 675-685
    • Lai, Z.C.1
  • 37
    • 70350414427 scopus 로고    scopus 로고
    • Two NDR kinase-MOB complexes function as distinct modules during septum formation and tip extension in Neurospora crassa
    • Maerz S, et al. 2009. Two NDR kinase-MOB complexes function as distinct modules during septum formation and tip extension in Neurospora crassa. Mol. Microbiol. 74:707-723.
    • (2009) Mol. Microbiol. , vol.74 , pp. 707-723
    • Maerz, S.1
  • 39
    • 52049115125 scopus 로고    scopus 로고
    • The nuclear Dbf2-related kinase COT1 and the mitogen-activated protein kinases MAK1 and MAK2 genetically interact to regulate filamentous growth, hyphal fusion and sexual development in Neurospora crassa
    • Maerz S, et al. 2008. The nuclear Dbf2-related kinase COT1 and the mitogen-activated protein kinases MAK1 and MAK2 genetically interact to regulate filamentous growth, hyphal fusion and sexual development in Neurospora crassa. Genetics 179:1313-1325.
    • (2008) Genetics , vol.179 , pp. 1313-1325
    • Maerz, S.1
  • 40
    • 0041472360 scopus 로고    scopus 로고
    • The Fungal Genetics Stock Center, from molds to molecules
    • McCluskey K. 2003. The Fungal Genetics Stock Center: from molds to molecules. Adv. Appl. Microbiol. 52:245-262.
    • (2003) Adv. Appl. Microbiol. , vol.52 , pp. 245-262
    • McCluskey, K.1
  • 41
    • 10744230793 scopus 로고    scopus 로고
    • RAM, a conserved signaling network that regulates Ace2p transcriptional activity and polarized morphogenesis
    • Nelson B, et al. 2003. RAM: a conserved signaling network that regulates Ace2p transcriptional activity and polarized morphogenesis. Mol. Biol. Cell 14:3782-3803.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3782-3803
    • Nelson, B.1
  • 42
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B, Taylor S, Ghosh G. 2004. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15:661-675.
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 43
    • 34547154729 scopus 로고    scopus 로고
    • Activation segment exchange: a common mechanism of kinase autophosphorylation? Trends Biochem
    • Oliver AW, Knapp S, Pearl LH. 2007. Activation segment exchange: a common mechanism of kinase autophosphorylation? Trends Biochem. Sci. 32:351-356.
    • (2007) Sci , vol.32 , pp. 351-356
    • Oliver, A.W.1    Knapp, S.2    Pearl, L.H.3
  • 44
    • 75649116876 scopus 로고    scopus 로고
    • Mutations in the C-terminus of the conserved NDR kinase, Cbk1p of Saccharomyces cerevisiae, make the protein independent of upstream activators
    • Panozzo C, Bourens M, Nowacka A, Herbert CJ. 2010. Mutations in the C-terminus of the conserved NDR kinase, Cbk1p of Saccharomyces cerevisiae, make the protein independent of upstream activators. Mol. Genet. Genomics 283:111-122.
    • (2010) Mol. Genet. Genomics , vol.283 , pp. 111-122
    • Panozzo, C.1    Bourens, M.2    Nowacka, A.3    Herbert, C.J.4
  • 46
    • 39449119544 scopus 로고    scopus 로고
    • Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites
    • Pike AC, et al. 2008. Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites. EMBO J. 27:704-714.
    • (2008) EMBO J , vol.27 , pp. 704-714
    • Pike, A.C.1
  • 47
    • 34249780407 scopus 로고    scopus 로고
    • The GCK II and III subfamilies of the STE20 group kinases
    • Pombo CM, et al. 2007. The GCK II and III subfamilies of the STE20 group kinases. Front. Biosci. 12:850-859.
    • (2007) Front. Biosci. , vol.12 , pp. 850-859
    • Pombo, C.M.1
  • 48
    • 3242794878 scopus 로고    scopus 로고
    • Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras
    • Praskova M, Khoklatchev A, Ortiz-Vega S, Avruch J. 2004. Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras. Biochem. J. 381:453-462.
    • (2004) Biochem. J. , vol.381 , pp. 453-462
    • Praskova, M.1    Khoklatchev, A.2    Ortiz-Vega, S.3    Avruch, J.4
  • 49
    • 40149111984 scopus 로고    scopus 로고
    • MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation
    • Praskova M, Xia F, Avruch J. 2008. MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation. Curr. Biol. 18:311-321.
    • (2008) Curr. Biol. , vol.18 , pp. 311-321
    • Praskova, M.1    Xia, F.2    Avruch, J.3
  • 50
    • 77957778865 scopus 로고    scopus 로고
    • Structural comparison of human mammalian ste20-like kinases
    • Record CJ, et al. 2010. Structural comparison of human mammalian ste20-like kinases. PLoS One 5:e11905.
    • (2010) PLoS One , vol.5
    • Record, C.J.1
  • 51
    • 79957860549 scopus 로고    scopus 로고
    • Architecture and development of the Neurospora crassa hypha: a model cell for polarized growth
    • Riquelme M, et al. 2011. Architecture and development of the Neurospora crassa hypha: a model cell for polarized growth. Fungal Biol. 115:446-474.
    • (2011) Fungal Biol , vol.115 , pp. 446-474
    • Riquelme, M.1
  • 52
    • 0345687346 scopus 로고    scopus 로고
    • The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa
    • Seiler S, Plamann M. 2003. The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa. Mol. Biol. Cell 14:4352-4364.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4352-4364
    • Seiler, S.1    Plamann, M.2
  • 53
    • 33748334318 scopus 로고    scopus 로고
    • The STE20/germinal center kinase POD6 interacts with the NDR kinase COT1 and is involved in polar tip extension in Neurospora crassa
    • Seiler S, Vogt N, Ziv C, Gorovits R, Yarden O. 2006. The STE20/germinal center kinase POD6 interacts with the NDR kinase COT1 and is involved in polar tip extension in Neurospora crassa. Mol. Biol. Cell 17:4080-4092.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4080-4092
    • Seiler, S.1    Vogt, N.2    Ziv, C.3    Gorovits, R.4    Yarden, O.5
  • 54
    • 2442700142 scopus 로고    scopus 로고
    • Critical role of T-loop and H-motif phosphorylation in the regulation of S6 kinase 1 by the tuberous sclerosis complex
    • Shah OJ, Hunter T. 2004. Critical role of T-loop and H-motif phosphorylation in the regulation of S6 kinase 1 by the tuberous sclerosis complex. J. Biol. Chem. 279:20816-20823.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20816-20823
    • Shah, O.J.1    Hunter, T.2
  • 55
    • 28544435761 scopus 로고    scopus 로고
    • Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3
    • Stegert MR, Hergovich A, Tamaskovic R, Bichsel SJ, Hemmings BA. 2005. Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3. Mol. Cell. Biol. 25:11019-11029.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 11019-11029
    • Stegert, M.R.1    Hergovich, A.2    Tamaskovic, R.3    Bichsel, S.J.4    Hemmings, B.A.5
  • 56
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker A, Newton AC. 2000. Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J. Biol. Chem. 275:8271-8274.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 57
    • 57649102412 scopus 로고    scopus 로고
    • NDR kinase is activated by RASSF1A/MST1 in response to Fas receptor stimulation and promotes apoptosis
    • Vichalkovski A, et al. 2008. NDR kinase is activated by RASSF1A/MST1 in response to Fas receptor stimulation and promotes apoptosis. Curr. Biol. 18:1889-1895.
    • (2008) Curr. Biol. , vol.18 , pp. 1889-1895
    • Vichalkovski, A.1
  • 58
    • 58149294002 scopus 로고    scopus 로고
    • The RHO1-specific GTPase-activating protein LRG1 regulates polar tip growth in parallel to Ndr kinase signaling in Neurospora
    • Vogt N, Seiler S. 2008. The RHO1-specific GTPase-activating protein LRG1 regulates polar tip growth in parallel to Ndr kinase signaling in Neurospora. Mol. Biol. Cell 19:4554-4569.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4554-4569
    • Vogt, N.1    Seiler, S.2
  • 59
    • 34247182696 scopus 로고    scopus 로고
    • Mob as tumor suppressor is activated by Hippo kinase for growth inhibition in Drosophila
    • Wei X, Shimizu T, Lai ZC. 2007. Mob as tumor suppressor is activated by Hippo kinase for growth inhibition in Drosophila.EMBOJ. 26:1772-1781.
    • (2007) EMBOJ , vol.26 , pp. 1772-1781
    • Wei, X.1    Shimizu, T.2    Lai, Z.C.3
  • 60
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang J, et al. 2002. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 9:940-944.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1
  • 61
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang J, et al. 2002. Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9:1227-1240.
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1
  • 62
    • 0026583041 scopus 로고
    • cot-1, a gene required for hyphal elongation in Neurospora crassa, encodes a protein kinase
    • Yarden O, Plamann M, Ebbole DJ, Yanofsky C. 1992. cot-1, a gene required for hyphal elongation in Neurospora crassa, encodes a protein kinase. EMBO J. 11:2159-2166.
    • (1992) EMBO J , vol.11 , pp. 2159-2166
    • Yarden, O.1    Plamann, M.2    Ebbole, D.J.3    Yanofsky, C.4
  • 63
    • 0034490689 scopus 로고    scopus 로고
    • Neuronal cell shape and neurite initiation are regulated by the Ndr kinase SAX-1, a member of the Orb6/COT-1/warts serine/threonine kinase family
    • Zallen JA, Peckol EL, Tobin DM, Bargmann CI. 2000. Neuronal cell shape and neurite initiation are regulated by the Ndr kinase SAX-1, a member of the Orb6/COT-1/warts serine/threonine kinase family. Mol. Biol. Cell 11:3177-3190.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3177-3190
    • Zallen, J.A.1    Peckol, E.L.2    Tobin, D.M.3    Bargmann, C.I.4
  • 64
    • 70449553042 scopus 로고    scopus 로고
    • Cell elongation and branching are regulated by differential phosphorylation states of the nuclear Dbf2-related kinase COT1 in Neurospora crassa
    • Ziv C, et al. 2009. Cell elongation and branching are regulated by differential phosphorylation states of the nuclear Dbf2-related kinase COT1 in Neurospora crassa. Mol. Microbiol. 74:974-989.
    • (2009) Mol. Microbiol. , vol.74 , pp. 974-989
    • Ziv, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.