메뉴 건너뛰기




Volumn 454, Issue 1, 2013, Pages 13-30

SOcK, MiSTs, MASK and STicKs: The GCKIII (germinal centre kinase III) kinases and their heterologous protein-protein interactions

Author keywords

Cytoskeleton; Focal adhesion; Germinal centre kinase III subfamily (GCKIII); Golgi; MO25; Protein phosphatase 2A (PP2A); Protein phosphorylation; STRAD (sterile 20 related kinase adaptor ); Striatin

Indexed keywords

CALMODULIN BINDING PROTEIN 3; CYTOPLASM PROTEIN; GERMINAL CENTRE KINASE III; GOLGIN A2; HETERODIMER; MAMMALIAN STE20 LIKE KINASE 3; MAMMALIAN STE20 LIKE KINASE 4; MITOGEN ACTIVATED PROTEIN KINASE; MO25 PROTEIN; MULTIPROTEIN COMPLEX; NERVE GROWTH FACTOR; OKADAIC ACID; PHOCEIN; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOTRANSFERASE; PROTEIN 14 3 3; PROTEIN KINASE; PROTEIN KINASE LKB1; REACTIVE OXYGEN METABOLITE; SCAFFOLD PROTEIN; SERINE; STE20 LIKE OXIDANT STRESS RESPONSE KINASE 1; STE20 RELATED KINASE ADAPTOR ALPHA; STRIATIN; THREONINE; TUBULIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84880859918     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130219     Document Type: Review
Times cited : (40)

References (151)
  • 1
    • 0035341895 scopus 로고    scopus 로고
    • The ste20 group kinases as regulators of map kinase cascades
    • Dan, I., Watanabe, N. M. and 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
  • 2
    • 68149089761 scopus 로고    scopus 로고
    • The mammalian family of sterile 20p-like protein kinases
    • Delpire, E. (2009) The mammalian family of sterile 20p-like protein kinases. Pfl̈ugers Arch. 458, 953-967.
    • (2009) Pfl̈ugers Arch , vol.458 , pp. 953-967
    • Delpire, E.1
  • 3
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. and Hunter, T. (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 5
    • 43049155951 scopus 로고    scopus 로고
    • Biosignaling of mammalian ste20-related kinases
    • Ling, P., Lu, T.-J., Yuan, C.-J. and Lai, M.-D. (2008) Biosignaling of mammalian Ste20-related kinases. Cell. Signalling 20, 1237-1247.
    • (2008) Cell. Signalling , vol.20 , pp. 1237-1247
    • Ling, P.1    Lu, T.-J.2    Yuan, C.-J.3    Lai, M.-D.4
  • 6
  • 8
    • 47049088906 scopus 로고    scopus 로고
    • Sok1 translocates from the golgi to the nucleus upon chemical anoxia and induces apoptotic cell death
    • Nogueira, A., Fidalgo, M., Molnar, A., Kyriakis, J., Force, T., Zalvide, J. and Pombo, C. M. (2008) SOK1 translocates from the Golgi to the nucleus upon chemical anoxia and induces apoptotic cell death. J. Biol. Chem. 283, 16248-16258.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16248-16258
    • Nogueira, A.1    Fidalgo, M.2    Molnar, A.3    Kyriakis, J.4    Force, T.5    Zalvide, J.6    Pombo, C.M.7
  • 9
    • 84860267857 scopus 로고    scopus 로고
    • Pdcd10 interacts with stk25 to accelerate cell apoptosis under oxidative stress
    • Zhang, H., Ma, X., Deng, X., Chen, Y., Mo, X., Zhang, Y., Zhao, H. and Ma, D. (2012) PDCD10 interacts with STK25 to accelerate cell apoptosis under oxidative stress. Front. Biosci. 17, 2295-2305.
    • (2012) Front. Biosci , vol.17 , pp. 2295-2305
    • Zhang, H.1    Ma, X.2    Deng, X.3    Chen, Y.4    Mo, X.5    Zhang, Y.6    Zhao, H.7    Ma, D.8
  • 10
    • 0029814060 scopus 로고    scopus 로고
    • Activation of a human ste20-like kinase by oxidant stress defines a novel stress response pathway
    • Pombo, C. M., Bonventre, J. V., Molnar, A., Kyriakis, J. and Force, T. (1996) Activation of a human Ste20-like kinase by oxidant stress defines a novel stress response pathway. EMBO J. 15, 4537-4546.
    • (1996) EMBO J. , vol.15 , pp. 4537-4546
    • Pombo, C.M.1    Bonventre, J.V.2    Molnar, A.3    Kyriakis, J.4    Force, T.5
  • 11
    • 0030925857 scopus 로고    scopus 로고
    • Ysk1, a novel mammalian protein kinase structurally related to ste20 and sps1, but is not involved in the known mapk pathways
    • Osada, S., Izawa, M., Saito, R., Mizuno, K., Suzuki, A., Hirai, S. and Ohno, S. (1997) YSK1, a novel mammalian protein kinase structurally related to Ste20 and SPS1, but is not involved in the known MAPK pathways. Oncogene 14, 2047-2057.
    • (1997) Oncogene , vol.14 , pp. 2047-2057
    • Osada, S.1    Izawa, M.2    Saito, R.3    Mizuno, K.4    Suzuki, A.5    Hirai, S.6    Ohno, S.7
  • 12
    • 0030657770 scopus 로고    scopus 로고
    • Cloning and characterization of a human ste20-like protein kinase with unusual cofactor requirements
    • Schinkmann, K. and Blenis, J. (1997) Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements. J. Biol. Chem. 272, 28695-28703.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28695-28703
    • Schinkmann, K.1    Blenis, J.2
  • 14
    • 0034723262 scopus 로고    scopus 로고
    • Identification of a human brain-specific isoform of mammalian ste20-like kinase 3 that is regulated by camp-dependent protein kinase
    • Zhou, T.-H., Ling, K., Guo, J., Zhou, H., Wu, Y.-L., Jing, Q., Ma, L. and Pei, G. (2000) Identification of a human brain-specific isoform of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent protein kinase. J. Biol. Chem. 275, 2513-2519.
    • (2000) J. Biol. Chem , vol.275 , pp. 2513-2519
    • Zhou, T.-H.1    Ling, K.2    Guo, J.3    Zhou, H.4    Wu, Y.-L.5    Jing, Q.6    Ma, L.7    Pei, G.8
  • 15
    • 0035933820 scopus 로고    scopus 로고
    • Cloning and characterization of mst4, a novel ste20-like kinase
    • Qian, Z., Lin, C., Espinosa, R., LeBeau, M. and Rosner, M. R. (2001) Cloning and characterization of MST4, a novel Ste20-like kinase. J. Biol. Chem. 276, 22439-22445.
    • (2001) J. Biol. Chem , vol.276 , pp. 22439-22445
    • Qian, Z.1    Lin, C.2    Espinosa, R.3    LeBeau, M.4    Rosner, M.R.5
  • 16
    • 0035807216 scopus 로고    scopus 로고
    • Mst4, a new ste20-related kinase that mediates cell growth and transformation via modulating erk pathway
    • Lin, J.-L., Chen, H.-C., Fang, H.-I., Robinson, D., Kung, H.-J. and Shih, H.-M. (2001) MST4, a new Ste20-related kinase that mediates cell growth and transformation via modulating ERK pathway. Oncogene 20, 6559-6569.
    • (2001) Oncogene , vol.20 , pp. 6559-6569
    • Lin, J.-L.1    Chen, H.-C.2    Fang, H.-I.3    Robinson, D.4    Kung, H.-J.5    Shih, H.-M.6
  • 17
    • 0038745407 scopus 로고    scopus 로고
    • The ste20 kinase mst4 plays a role in prostate cancer progression
    • Sung, V., Luo, W., Qian, D., Lee, I., Jallal, B. and Gishizky, M. (2003) The Ste20 kinase MST4 plays a role in prostate cancer progression. Cancer Res. 63, 3356-3363.
    • (2003) Cancer Res. , vol.63 , pp. 3356-3363
    • Sung, V.1    Luo, W.2    Qian, D.3    Lee, I.4    Jallal, B.5    Gishizky, M.6
  • 21
    • 4143118028 scopus 로고    scopus 로고
    • Identification and characterization of the nuclear import and export signals of the mammalian ste20-like protein kinase 3
    • Lee, W.-S., Hsu, C.-Y., Wang, P.-L., Huang, C.-Y. F., Chang, C.-H. and Yuan, C.-J. (2004) Identification and characterization of the nuclear import and export signals of the mammalian Ste20-like protein kinase 3. FEBS Lett. 572, 41-45.
    • (2004) FEBS Lett. , vol.572 , pp. 41-45
    • Lee, W.-S.1    Hsu, C.-Y.2    Wang, P.-L.3    Huang, C.-Y.F.4    Chang, C.-H.5    Yuan, C.-J.6
  • 22
    • 66349137330 scopus 로고    scopus 로고
    • Functional analyses of human and zebrafish 18-Amino acid in-frame deletion pave the way for domain mapping of the cerebral cavernous malformation 3 protein
    • Voss, K., Stahl, S., Hogan, B. M., Reinders, J., Schleider, E., Schulte-Merker, S. and Felbor, U. (2009) Functional analyses of human and zebrafish 18-Amino acid in-frame deletion pave the way for domain mapping of the cerebral cavernous malformation 3 protein. Hum. Mutat. 30, 1003-1011.
    • (2009) Hum. Mutat. , vol.30 , pp. 1003-1011
    • Voss, K.1    Stahl, S.2    Hogan, B.M.3    Reinders, J.4    Schleider, E.5    Schulte-Merker, S.6    Felbor, U.7
  • 24
    • 77954926292 scopus 로고    scopus 로고
    • Crystal structure of ccm3, a cerebral cavernous malformation protein critical for vascular integrity
    • Li, X., Zhang, R., Zhang, H., He, Y., Ji, W., Min, W. and Boggon, T. J. (2010) Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity. J. Biol. Chem. 285, 24099-24107.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24099-24107
    • Li, X.1    Zhang, R.2    Zhang, H.3    He, Y.4    Ji, W.5    Min, W.6    Boggon, T.J.7
  • 25
    • 77956262153 scopus 로고    scopus 로고
    • Crystal structure of human programmed cell death 10 complexed with inositol-(1, 3, 4, 5)-tetrakisphosphate: A novel adaptor protein involved in human cerebral cavernous malformation
    • Ding, J., Wang, X., Li, D.-F., Hu, Y., Zhang, Y. and Wang, D.-C. (2010) Crystal structure of human programmed cell death 10 complexed with inositol-(1, 3, 4, 5)-tetrakisphosphate: A novel adaptor protein involved in human cerebral cavernous malformation. Biochem. Biophys. Res. Commun. 399, 587-592.
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 587-592
    • Ding, J.1    Wang, X.2    Li, D.-F.3    Hu, Y.4    Zhang, Y.5    Wang, D.-C.6
  • 27
    • 34250330782 scopus 로고    scopus 로고
    • Pdcd10 interacts with ste20-related kinase mst4 to promote cell growth and transformation via modulation of the erk pathway
    • Ma, X., Zhao, H., Shan, J., Long, F., Chen, Y., Chen, Y., Zhang, Y., Han, X. and Ma, D. (2007) PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway. Mol. Biol. Cell 18, 1965-1978.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1965-1978
    • Ma, X.1    Zhao, H.2    Shan, J.3    Long, F.4    Chen, Y.5    Chen, Y.6    Zhang, Y.7    Han, X.8    Ma, D.9
  • 28
    • 34948833449 scopus 로고    scopus 로고
    • Ccm3 interacts with ccm2 indicating common pathogenesis for cerebral cavernous malformations
    • Voss, K., Stahl, S., Schleider, E., Ullrich, S., Nickel, J., Mueller, T. D. and Felbor, U. (2007) CCM3 interacts with CCM2 indicating common pathogenesis for cerebral cavernous malformations. Neurogenetics 8, 249-256.
    • (2007) Neurogenetics , vol.8 , pp. 249-256
    • Voss, K.1    Stahl, S.2    Schleider, E.3    Ullrich, S.4    Nickel, J.5    Mueller, T.D.6    Felbor, U.7
  • 29
    • 77951194603 scopus 로고    scopus 로고
    • Ccm3/pdcd10 stabilizes gckiii proteins to promote golgi assembly and cell orientation
    • Fidalgo, M., Fraile, M., Pires, A., Force, T., Pombo, C. and Zalvide, J. (2010) CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation. J. Cell Sci. 123, 1274-1284.
    • (2010) J. Cell Sci. , vol.123 , pp. 1274-1284
    • Fidalgo, M.1    Fraile, M.2    Pires, A.3    Force, T.4    Pombo, C.5    Zalvide, J.6
  • 31
    • 84863483803 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic studies of ccm3 in complex with the c-terminal domain of mst4
    • Xu, X., Wang, X., Ding, J. and Wang, D.-C. (2012) Crystallization and preliminary crystallographic studies of CCM3 in complex with the C-terminal domain of MST4. Acta Crystallogr., Sect. F: Struct. Biol. Crystal. Commun. 68, 760-763.
    • (2012) Acta Crystallogr., Sect. F: Struct. Biol. Crystal. Commun , vol.68 , pp. 760-763
    • Xu, X.1    Wang, X.2    Ding, J.3    Wang, D.-C.4
  • 32
    • 0030703639 scopus 로고    scopus 로고
    • Activation of the ste20-like oxidant stress response kinase-1 during the initial stages of chemical anoxia-induced necrotic cell death. Requirement for dual inputs of oxidant stress and increased cytosolic [ca2+ ]
    • Pombo, C. M., Tsujita, T., Kyriakis, J. M., Bonventre, J. V. and Force, T. (1997) Activation of the Ste20-like oxidant stress response kinase-1 during the initial stages of chemical anoxia-induced necrotic cell death. Requirement for dual inputs of oxidant stress and increased cytosolic [Ca2+ ]. J. Biol. Chem. 272, 29372-29379.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29372-29379
    • Pombo, C.M.1    Tsujita, T.2    Kyriakis, J.M.3    Bonventre, J.V.4    Force, T.5
  • 33
    • 84859501932 scopus 로고    scopus 로고
    • Adaptor protein cerebral cavernous malformation 3 (ccm3) mediates phosphorylation of the cytoskeletal proteins ezrin/radixin/moesin by mammalian ste20-4 to protect cells from oxidative stress
    • Fidalgo, M., Guerrero, A., Fraile, M., Iglesias, C., Pombo, C. M. and Zalvide, J. (2012) Adaptor protein cerebral cavernous malformation 3 (CCM3) mediates phosphorylation of the cytoskeletal proteins ezrin/radixin/moesin by mammalian Ste20-4 to protect cells from oxidative stress. J. Biol. Chem. 287, 11556-11565.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11556-11565
    • Fidalgo, M.1    Guerrero, A.2    Fraile, M.3    Iglesias, C.4    Pombo, C.M.5    Zalvide, J.6
  • 34
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (egf)-induced generation of hydrogen peroxide. Role in egf-receptor-mediated tyrosine phosphorylation
    • Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I. C., Tekle, E., Chock, P. B. and Rhee, S. G. (1997) Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF-receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272, 217-221.
    • (1997) J. Biol. Chem. , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 35
    • 33845989128 scopus 로고    scopus 로고
    • Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (mst3) involves paxillin and protein-tyrosine phosphatase-pest
    • Lu, T.-J., Lai, W.-Y., Huang, C.-Y. F., Hsieh, W.-J., Yu, J.-S., Hsieh, Y.-J., Chang, W.-T., Leu, T.-H., Chang, W.-C., Chuang, W.-J. et al. (2006) Inhibition of cell migration by autophosphorylated mammalian Sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST. J. Biol. Chem. 281, 38405-38417.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38405-38417
    • Lu, T.-J.1    Lai, W.-Y.2    Huang, C.-Y.F.3    Hsieh, W.-J.4    Yu, J.-S.5    Hsieh, Y.-J.6    Chang, W.-T.7    Leu, T.-H.8    Chang, W.-C.9    Chuang, W.-J.10
  • 36
    • 1842613600 scopus 로고    scopus 로고
    • Ysk1 is activated by the golgi matrix protein gm130 and plays a role in cell migration through its substrate 14-3-3
    • Preisinger, C., Short, B., De Corte, V., Bruyneel, E., Haas, A., Kopajtich, R., Gettemans, J. and Barr, F. A. (2004) YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3ζ. J. Cell Biol. 164, 1009-1020.
    • (2004) J. Cell Biol , vol.164 , pp. 1009-1020
    • Preisinger, C.1    Short, B.2    De Corte, V.3    Bruyneel, E.4    Haas, A.5    Kopajtich, R.6    Gettemans, J.7    Barr, F.A.8
  • 37
    • 80053604188 scopus 로고    scopus 로고
    • Protein phosphatase 2a (pp2a) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian ste20-like kinase mst3
    • Gordon, J., Hwang, J., Carrier, K. J., Jones, C. A., Kern, Q. L., Moreno, C. S., Karas, R. H. and Pallas, D. C. (2011) Protein phosphatase 2a (PP2A) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian Ste20-like kinase Mst3. BMC Biochem. 12, 54.
    • (2011) BMC Biochem , vol.12 , pp. 54
    • Gordon, J.1    Hwang, J.2    Carrier, K.J.3    Jones, C.A.4    Kern, Q.L.5    Moreno, C.S.6    Karas, R.H.7    Pallas, D.C.8
  • 38
    • 84862511427 scopus 로고    scopus 로고
    • Comparative kinome analysis to identify putative colon tumor biomarkers
    • Hennig, E. E., Mikula, M., Rubel, T., Dadlez, M. and Ostrowski, J. (2012) Comparative kinome analysis to identify putative colon tumor biomarkers. J. Mol. Med. 90, 447-456.
    • (2012) J. Mol. Med. , vol.90 , pp. 447-456
    • Hennig, E.E.1    Mikula, M.2    Rubel, T.3    Dadlez, M.4    Ostrowski, J.5
  • 39
    • 78049288601 scopus 로고    scopus 로고
    • Signal transduction protein array analysis links lrrk2 to ste20 kinases and pkcζ that modulate neuronal plasticity
    • Zach, S., Felk, S. and Gillardon, F. (2010) Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKCζ that modulate neuronal plasticity. PLoS ONE 5, e13191.
    • (2010) PLoS ONE , vol.5
    • Zach, S.1    Felk, S.2    Gillardon, F.3
  • 40
    • 27744593477 scopus 로고    scopus 로고
    • A single pair of acidic residues in the kinase major groove mediates strong substrate preference for p-2 or p-5 arginine in the agc, camk, and ste kinase families
    • Zhu, G., Fujii, K., Liu, Y., Codrea, V., Herrero, J. and Shaw, S. (2005) A single pair of acidic residues in the kinase major groove mediates strong substrate preference for P-2 or P-5 arginine in the AGC, CAMK, and STE kinase families. J. Biol. Chem. 280, 36372-36379.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36372-36379
    • Zhu, G.1    Fujii, K.2    Liu, Y.3    Codrea, V.4    Herrero, J.5    Shaw, S.6
  • 41
    • 79953187537 scopus 로고    scopus 로고
    • Mammalian ste20-like protein kinase 3 plays a role in hypoxia-induced apoptosis of trophoblast cell line 3a-sub-e
    • Wu, H.-Y., Lin, C.-Y., Chen, T.-C., Pan, S.-T. and Yuan, C.-J. (2011) Mammalian Ste20-like protein kinase 3 plays a role in hypoxia-induced apoptosis of trophoblast cell line 3A-sub-E. Int. J. Biochem. Cell Biol. 43, 742-750.
    • (2011) Int. J. Biochem. Cell Biol , vol.43 , pp. 742-750
    • Wu, H.-Y.1    Lin, C.-Y.2    Chen, T.-C.3    Pan, S.-T.4    Yuan, C.-J.5
  • 42
    • 84856290771 scopus 로고    scopus 로고
    • The centrosome in cells and organisms
    • Bornens, M. (2012) The centrosome in cells and organisms. Science 335, 422-266.
    • (2012) Science , vol.335 , pp. 266-422
    • Bornens, M.1
  • 43
    • 84876176354 scopus 로고    scopus 로고
    • Q&a: Who needs a centrosome?
    • Bettencourt-Dias, M. (2013) Q&A: who needs a centrosome? BMC Biol. 11, 28.
    • (2013) BMC Biol. , vol.11 , pp. 28
    • Bettencourt-Dias, M.1
  • 44
    • 84855602576 scopus 로고    scopus 로고
    • Interplay between microtubule dynamics and intracellular organization
    • de Forges, H., Bouissou, A. and Perez, F. (2012) Interplay between microtubule dynamics and intracellular organization. Int. J. Biochem. Cell Biol. 44, 266-274.
    • (2012) Int. J. Biochem. Cell Biol , vol.44 , pp. 266-274
    • De Forges, H.1    Bouissou, A.2    Perez, F.3
  • 45
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of cdc42 controls cell polarity in migrating astrocytes through pkc
    • Etienne-Manneville, S. and Hall, A. (2001) Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCζ. Cell 106, 489-498.
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 46
    • 84862323152 scopus 로고    scopus 로고
    • The golgi in cell migration: Regulation by signal transduction and its implications for cancer cell metastasis
    • Millarte, V. and Farhan, H. (2012) The Golgi in cell migration: regulation by signal transduction and its implications for cancer cell metastasis. Sci. World J. 2012, 498278.
    • (2012) Sci. World J. , vol.2012 , pp. 498278
    • Millarte, V.1    Farhan, H.2
  • 48
    • 77950634328 scopus 로고    scopus 로고
    • Emerging new roles of gm130, a cis-golgi matrix protein, in higher order cell functions
    • Nakamura, N. (2010) Emerging new roles of GM130, a cis-Golgi matrix protein, in higher order cell functions. J. Pharmacol. Sci. 112, 255-264.
    • (2010) J. Pharmacol. Sci. , vol.112 , pp. 255-264
    • Nakamura, N.1
  • 50
    • 67651215903 scopus 로고    scopus 로고
    • Serine 58 of 14-3-3ζ is a molecular switch regulating ask1 and oxidant stress-induced cell death
    • Zhou, J., Shao, Z., Kerkela, R., Ichijo, H., Muslin, A. J., Pombo, C. and Force, T. (2009) Serine 58 of 14-3-3ζ is a molecular switch regulating ASK1 and oxidant stress-induced cell death. Mol. Cell. Biol. 29, 4167-4176.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 4167-4176
    • Zhou, J.1    Shao, Z.2    Kerkela, R.3    Ichijo, H.4    Muslin, A.J.5    Pombo, C.6    Force, T.7
  • 51
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C., Cantley, L.C. and Yaffe, M. B. (2003) Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 3635-3641.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 52
    • 0034050449 scopus 로고    scopus 로고
    • Wd40 repeat proteins striatin and s/g2 nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2a
    • Moreno, C. S., Park, S., Nelson, K., Ashby, D., Hubalek, F., Lane, W. S. and Pallas, D. C. (2000) WD40 repeat proteins striatin and S/G2 nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. J. Biol. Chem. 275, 5257-5263.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5257-5263
    • Moreno, C.S.1    Park, S.2    Nelson, K.3    Ashby, D.4    Hubalek, F.5    Lane, W.S.6    Pallas, D.C.7
  • 54
    • 58549085778 scopus 로고    scopus 로고
    • An integrated workflow for charting the human interaction proteome: Insights into the pp2a system
    • Glatter, T., Wepf, A., Aebersold, R. and Gstaiger, M. (2009) An integrated workflow for charting the human interaction proteome: insights into the PP2A system. Mol. Syst. Biol. 5, 237.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 237
    • Glatter, T.1    Wepf, A.2    Aebersold, R.3    Gstaiger, M.4
  • 55
    • 59149096171 scopus 로고    scopus 로고
    • A pp2a phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (ccm3) protein
    • Goudreault, M., D'Ambrosio, L. M., Kean, M. J., Mullin, M. J., Larsen, B. G., Sanchez, A., Chaudhry, S., Chen, G. I., Sicheri, F., Nesvizhskii, A. I. et al. (2009) A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein. Mol. Cell. Proteomics 8, 157-171.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 157-171
    • Goudreault, M.1    D'Ambrosio, L.M.2    Kean, M.J.3    Mullin, M.J.4    Larsen, B.G.5    Sanchez, A.6    Chaudhry, S.7    Chen, G.I.8    Sicheri, F.9    Nesvizhskii, A.I.10
  • 56
    • 84864111171 scopus 로고    scopus 로고
    • Misshapen-like kinase 1 (mink1) is a novel component of striatin-interacting phosphatase and kinase (stripak) and is required for the completion of cytokinesis
    • Hyodo, T., Ito, S., Hasegawa, H., Asano, E., Maeda, M., Urano, T., Takahashi, M., Hamaguchi, M. and Senga, T. (2012) Misshapen-like kinase 1 (MINK1) is a novel component of striatin-interacting phosphatase and kinase (STRIPAK) and is required for the completion of cytokinesis. J. Biol. Chem. 287, 25019-25029.
    • (2012) J. Biol. Chem. , vol.287 , pp. 25019-25029
    • Hyodo, T.1    Ito, S.2    Hasegawa, H.3    Asano, E.4    Maeda, M.5    Urano, T.6    Takahashi, M.7    Hamaguchi, M.8    Senga, T.9
  • 58
    • 0035968296 scopus 로고    scopus 로고
    • A mammalian homolog of yeast mob1 is both a member and a putative substrate of striatin family-protein phosphatase 2a complexes
    • Moreno, C. S., Lane, W. S. and Pallas, D. C. (2001) A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes. J. Biol. Chem. 276, 24253-24260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24253-24260
    • Moreno, C.S.1    Lane, W.S.2    Pallas, D.C.3
  • 59
    • 0028959481 scopus 로고
    • A cell-cycle nuclear autoantigen containing wd-40 motifs expressed mainly in s and g2 phase cells
    • Muro, Y., Chan, E. K. L., Landberg, G. and Tan, E. M. (1995) A cell-cycle nuclear autoantigen containing WD-40 motifs expressed mainly in S and G2 phase cells. Biochem. Biophys. Res. Commun. 207, 1029-1037.
    • (1995) Biochem. Biophys. Res. Commun , vol.207 , pp. 1029-1037
    • Muro, Y.1    Chan, E.K.L.2    Landberg, G.3    Tan, E.M.4
  • 60
    • 33645037097 scopus 로고    scopus 로고
    • The striatin family: A new signaling platform in dendritic spines
    • Benoist, M., Gaillard, S. and Castets, F. (2006) The striatin family: A new signaling platform in dendritic spines. J. Physiol. 99, 146-153.
    • (2006) J. Physiol , vol.99 , pp. 146-153
    • Benoist, M.1    Gaillard, S.2    Castets, F.3
  • 62
    • 0034733727 scopus 로고    scopus 로고
    • Zinedin, sg2na, and striatin are calmodulin-binding, wd repeat proteins principally expressed in the brain
    • Castets, F., Rakitina, T., Gaillard, S., Moqrich, A., Mattei, M.-G. and Monneron, A. (2000) Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain. J. Biol. Chem. 275, 19970-19977.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19970-19977
    • Castets, F.1    Rakitina, T.2    Gaillard, S.3    Moqrich, A.4    Mattei, M.-G.5    Monneron, A.6
  • 63
    • 77955287380 scopus 로고    scopus 로고
    • Ccm3 signaling through sterile 20-like kinases plays an essential role during zebrafish cardiovascular development and cerebral cavernous malformations
    • Zheng, X., Xu, C., Di Lorenzo, A., Kleaveland, B., Zou, Z., Seiler, C., Chen, M., Cheng, L., Xiao, J., He, J. et al. (2010) CCM3 signaling through sterile 20-like kinases plays an essential role during zebrafish cardiovascular development and cerebral cavernous malformations. J. Clin. Invest. 120, 2795-2804.
    • (2010) J. Clin. Invest. , vol.120 , pp. 2795-2804
    • Zheng, X.1    Xu, C.2    Di Lorenzo, A.3    Kleaveland, B.4    Zou, Z.5    Seiler, C.6    Chen, M.7    Cheng, L.8    Xiao, J.9    He, J.10
  • 64
    • 84856107059 scopus 로고    scopus 로고
    • Ccm3 functions in a manner distinct from ccm1 and ccm2 in a zebrafish model of ccm vascular disease
    • Yoruk, B., Gillers, B. S., Chi, N. C. and Scott, I. C. (2012) Ccm3 functions in a manner distinct from Ccm1 and Ccm2 in a zebrafish model of CCM vascular disease. Dev. Biol. 362, 121-131.
    • (2012) Dev. Biol , vol.362 , pp. 121-131
    • Yoruk, B.1    Gillers, B.S.2    Chi, N.C.3    Scott, I.C.4
  • 65
    • 76349124651 scopus 로고    scopus 로고
    • Recent insights into cerebral cavernous malformations: The molecular genetics of ccm
    • Riant, F., Bergametti, F., Ayrignac, X., Boulday, G. and Tournier-Lasserve, E. (2010) Recent insights into cerebral cavernous malformations: The molecular genetics of CCM. FEBS J. 277, 1070-1075.
    • (2010) FEBS J. , vol.277 , pp. 1070-1075
    • Riant, F.1    Bergametti, F.2    Ayrignac, X.3    Boulday, G.4    Tournier-Lasserve, E.5
  • 66
    • 76349106156 scopus 로고    scopus 로고
    • Recent insights into cerebral cavernous malformations: Animal models of CCM and the human phenotype
    • Chan, A. C., Li, D. Y., Berg, M. J. and Whitehead, K. J. (2010) Recent insights into cerebral cavernous malformations: Animal models of CCM and the human phenotype. FEBS J. 277, 1076-1083.
    • (2010) FEBS J. , vol.277 , pp. 1076-1083
    • Chan, A.C.1    Li, D.Y.2    Berg, M.J.3    Whitehead, K.J.4
  • 67
    • 76349109226 scopus 로고    scopus 로고
    • Recent insights into cerebral cavernous malformations: A complex jigsaw puzzle under construction
    • Faurobert, E. and Albiges-Rizo, C. (2010) Recent insights into cerebral cavernous malformations: A complex jigsaw puzzle under construction. FEBS J. 277, 1084-1096.
    • (2010) FEBS J. , vol.277 , pp. 1084-1096
    • Faurobert, E.1    Albiges-Rizo, C.2
  • 69
    • 24144454827 scopus 로고    scopus 로고
    • Ccm1 and ccm2 protein interactions in cell signaling: Implications for cerebral cavernous malformations pathogenesis
    • Zawistowski, J. S., Stalheim, L., Uhlik, M. T., Abell, A. N., Ancrile, B. B., Johnson, G. L. and Marchuk, D. A. (2005) CCM1 and CCM2 protein interactions in cell signaling: implications for cerebral cavernous malformations pathogenesis. Hum. Mol. Genet. 14, 2521-2531.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2521-2531
    • Zawistowski, J.S.1    Stalheim, L.2    Uhlik, M.T.3    Abell, A.N.4    Ancrile, B.B.5    Johnson, G.L.6    Marchuk, D.A.7
  • 70
    • 79960397998 scopus 로고    scopus 로고
    • Molecular recognition of leucine-Aspartate repeat (ld) motifs by the focal adhesion targeting homology domain of cerebral cavernous malformation 3 (ccm3)
    • Li, X., Ji, W., Zhang, R., Folta-Stogniew, E., Min, W. and Boggon, T. J. (2011) Molecular recognition of leucine-Aspartate repeat (LD) motifs by the focal adhesion targeting homology domain of cerebral cavernous malformation 3 (CCM3). J. Biol. Chem. 286, 26138-26147.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26138-26147
    • Li, X.1    Ji, W.2    Zhang, R.3    Folta-Stogniew, E.4    Min, W.5    Boggon, T.J.6
  • 71
    • 0035172754 scopus 로고    scopus 로고
    • Molecular cloning and characterization of phocein, a protein found from the golgi complex to dendritic spines
    • Baillat, G., Moqrich, A., Castets, F., Baude, A., Bailly, Y., Benmerah, A. and Monneron, A. (2001) Molecular cloning and characterization of phocein, a protein found from the Golgi complex to dendritic spines. Mol. Biol. Cell 12, 663-673.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 663-673
    • Baillat, G.1    Moqrich, A.2    Castets, F.3    Baude, A.4    Bailly, Y.5    Benmerah, A.6    Monneron, A.7
  • 72
    • 61649127812 scopus 로고    scopus 로고
    • From promiscuity to precision: Protein phosphatases get a makeover
    • Virshup, D. M. and Shenolikar, S. (2009) From promiscuity to precision: protein phosphatases get a makeover. Mol. Cell 33, 537-545.
    • (2009) Mol. Cell , vol.33 , pp. 537-545
    • Virshup, D.M.1    Shenolikar, S.2
  • 73
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi, Y. (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139, 468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 74
    • 82755163057 scopus 로고    scopus 로고
    • Determinants for substrate specificity of protein phosphatase 2A
    • Slupe, A. M., Merrill, R. A. and Strack, S. (2011) Determinants for substrate specificity of protein phosphatase 2A. Enzyme Res. 2011, 398751.
    • (2011) Enzyme Res. , vol.2011 , pp. 398751
    • Slupe, A.M.1    Merrill, R.A.2    Strack, S.3
  • 75
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • Deakin, N. O. and Turner, C. E. (2008) Paxillin comes of age. J. Cell Sci. 121, 2435-2444.
    • (2008) J. Cell Sci. , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 76
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger, D. S. and Calderwood, D. A. (2009) Integrin signalling at a glance. J. Cell Sci. 122, 159-163.
    • (2009) J. Cell Sci. , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 77
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of pak-interacting exchange factor pix to git1 promotes focal complex disassembly
    • Zhao, Z. S., Manser, E., Loo, T. H. and Lim, L. (2000) Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol. Cell. Biol. 20, 6354-6363.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6354-6363
    • Zhao, Z.S.1    Manser, E.2    Loo, T.H.3    Lim, L.4
  • 78
    • 0028129146 scopus 로고
    • Ptp-pest: A protein tyrosine phosphatase regulated by serine phosphorylation
    • Garton, A. J. and Tonks, N. K. (1994) PTP-PEST: A protein tyrosine phosphatase regulated by serine phosphorylation. EMBO J. 13, 3763-3771.
    • (1994) EMBO J. , vol.13 , pp. 3763-3771
    • Garton, A.J.1    Tonks, N.K.2
  • 79
    • 79953720901 scopus 로고    scopus 로고
    • Downregulation of sok1 promotes the migration of mcf-7 cells
    • Chen, X.-D. and Cho, C.-Y. (2011) Downregulation of SOK1 promotes the migration of MCF-7 cells. Biochem. Biophys. Res. Commun. 407, 389-392.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 389-392
    • Chen, X.-D.1    Cho, C.-Y.2
  • 81
    • 79960733700 scopus 로고    scopus 로고
    • Ezrin, radixin and moesin: Key regulators of membrane-cortex interactions and signaling
    • Neisch, A. L. and Fehon, R. G. (2011) Ezrin, radixin and moesin: key regulators of membrane-cortex interactions and signaling. Curr. Opin. Cell Biol. 23, 377-382.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 377-382
    • Neisch, A.L.1    Fehon, R.G.2
  • 84
    • 0027393155 scopus 로고
    • Molecular cloning of a novel mrna sequence expressed in cleavage stage mouse embryos
    • Miyamoto, H., Matsushiro, A. and Nozaki, M. (1993) Molecular cloning of a novel mRNA sequence expressed in cleavage stage mouse embryos. Mol. Reprod. Dev. 34, 1-7.
    • (1993) Mol. Reprod. Dev. , vol.34 , pp. 1-7
    • Miyamoto, H.1    Matsushiro, A.2    Nozaki, M.3
  • 85
    • 0030002157 scopus 로고    scopus 로고
    • Molecular characterization of the drosophila mo25 gene, which is conserved among drosophila, mouse, and yeast
    • Nozaki, M., Onishi, Y., Togashi, S. and Miyamoto, H. (1996) Molecular characterization of the Drosophila Mo25 gene, which is conserved among Drosophila, mouse, and yeast. DNA Cell Biol. 15, 505-509.
    • (1996) DNA Cell Biol. , vol.15 , pp. 505-509
    • Nozaki, M.1    Onishi, Y.2    Togashi, S.3    Miyamoto, H.4
  • 88
    • 84858782079 scopus 로고    scopus 로고
    • Ampk: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie, D. G., Ross, F. A. and Hawley, S. A. (2012) AMPK: A nutrient and energy sensor that maintains energy homeostasis. Nat. Rev. Mol. Cell Biol. 13, 251-262.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 89
    • 72949115493 scopus 로고    scopus 로고
    • Structure of the lkb1-strad-mo25 complex reveals an allosteric mechanism of kinase activation
    • Zeqiraj, E., Filippi, B. M., Deak, M., Alessi, D. R. and van Aalten, D. M. F. (2009) Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation. Science 326, 1707-1711.
    • (2009) Science , vol.326 , pp. 1707-1711
    • Zeqiraj, E.1    Filippi, B.M.2    Deak, M.3    Alessi, D.R.4    Van Aalten, D.M.F.5
  • 90
    • 67649950358 scopus 로고    scopus 로고
    • Atp and mo25α regulate the conformational state of the stradα pseudokinase and activation of the lkb1 tumour suppressor
    • Zeqiraj, E., Filippi, B. M., Goldie, S., Navratilova, I., Boudeau, J., Deak, M., Alessi, D. R. and van Aalten, D. M. F. (2009) ATP and MO25α regulate the conformational state of the STRADα pseudokinase and activation of the LKB1 tumour suppressor. PLoS Biol. 7, e1000126.
    • (2009) PLoS Biol. , vol.7
    • Zeqiraj, E.1    Filippi, B.M.2    Goldie, S.3    Navratilova, I.4    Boudeau, J.5    Deak, M.6    Alessi, D.R.7    Van Aalten, D.M.F.8
  • 94
    • 83755225807 scopus 로고    scopus 로고
    • Functional insights into the activation mechanism of ste20-related kinases
    • Gagnon, K. B., Rios, K. and Delpire, E. (2011) Functional insights into the activation mechanism of Ste20-related kinases. Cell. Physiol. Biochem. 28, 1219-1230.
    • (2011) Cell. Physiol. Biochem , vol.28 , pp. 1219-1230
    • Gagnon, K.B.1    Rios, K.2    Delpire, E.3
  • 95
    • 2942729619 scopus 로고    scopus 로고
    • Lkb1 tumor suppressor protein: Partaker in cell polarity
    • Baas, A. F., Smit, L. and Clevers, H. (2004) LKB1 tumor suppressor protein: PARtaker in cell polarity. Trends Cell Biol. 14, 312-319.
    • (2004) Trends Cell Biol. , vol.14 , pp. 312-319
    • Baas, A.F.1    Smit, L.2    Clevers, H.3
  • 96
    • 1542777034 scopus 로고    scopus 로고
    • Complete polarization of single intestinal epithelial cells upon activation of lkb1 by strad
    • Koerten, H. K., Peters, P. J. and Clevers, H. C. (2004) Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD. Cell 116, 457-466.
    • (2004) Cell , vol.116 , pp. 457-466
    • Koerten, H.K.1    Peters, P.J.2    Clevers, H.C.3
  • 97
    • 79955717277 scopus 로고    scopus 로고
    • Role of lkb1-sad/mark pathway in neuronal polarization
    • Shelly, M. and Poo, M.-M. (2011) Role of LKB1-SAD/MARK pathway in neuronal polarization. Develop. Neurobiol. 71, 508-527.
    • (2011) Develop. Neurobiol , vol.71 , pp. 508-527
    • Shelly, M.1    Poo, M.-M.2
  • 98
    • 84861325586 scopus 로고    scopus 로고
    • Par-1/mark: A kinase essential for maintaining the dynamic state of microtubules
    • Hayashi, K., Suzuki, A. and Ohno, S. (2012) PAR-1/MARK: A kinase essential for maintaining the dynamic state of microtubules. Cell Struct. Funct. 37, 21-25.
    • (2012) Cell Struct. Funct , vol.37 , pp. 21-25
    • Hayashi, K.1    Suzuki, A.2    Ohno, S.3
  • 101
    • 0041488911 scopus 로고    scopus 로고
    • Trk receptors: Roles in neuronal signal transduction
    • Huang, E. J. and Reichardt, L. F. (2003) Trk receptors: roles in neuronal signal transduction. Annu. Rev. Biochem. 72, 609-642.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 609-642
    • Huang, E.J.1    Reichardt, L.F.2
  • 102
    • 77949721758 scopus 로고    scopus 로고
    • Neurotrophin receptors: Old friends with new partners
    • Schecterson, L. C. and Bothwell, M. (2010) Neurotrophin receptors: old friends with new partners. Develop. Neurobiol. 70, 332-338.
    • (2010) Develop. Neurobiol , vol.70 , pp. 332-338
    • Schecterson, L.C.1    Bothwell, M.2
  • 103
    • 0016830798 scopus 로고
    • Nerve growth factor-induced process formation by cultured rat pheochromocytoma cells
    • Tischler, A. S. and Greene, L. A. (1975) Nerve growth factor-induced process formation by cultured rat pheochromocytoma cells. Nature 258, 341-342.
    • (1975) Nature , vol.258 , pp. 341-342
    • Tischler, A.S.1    Greene, L.A.2
  • 104
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L. A. and Tischler, A. S. (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 73, 2424-2428.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 105
    • 0023054111 scopus 로고
    • Regulation of protein kinase activities in pc12 pheochromocytoma cells
    • Blenis, J. and Erikson, R. L. (1986) Regulation of protein kinase activities in PC12 pheochromocytoma cells. EMBO J. 5, 3441-3447.
    • (1986) EMBO J. , vol.5 , pp. 3441-3447
    • Blenis, J.1    Erikson, R.L.2
  • 106
    • 0023644969 scopus 로고
    • Cell-free detection and characterization of a novel nerve growth factor-Activated protein kinase in pc12 cells
    • Rowland, E. A., M̈uller, T. H., Goldstein, M. and Greene, L. A. (1987) Cell-free detection and characterization of a novel nerve growth factor-Activated protein kinase in PC12 cells. J. Biol. Chem. 262, 7504-7513.
    • (1987) J. Biol. Chem , vol.262 , pp. 7504-7513
    • Rowland, E.A.1    M̈uller, T.H.2    Goldstein, M.3    Greene, L.A.4
  • 107
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of pkn, a protein kinase having a catalytic domain homologous to that of pkc
    • Mukai, H. (2003) The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC. J. Biochem. 133, 17-27.
    • (2003) J. Biochem. , vol.133 , pp. 17-27
    • Mukai, H.1
  • 108
    • 0026802101 scopus 로고
    • Nerve growth factor-Activated protein kinase n. Characterization and rapid near homogeneity purification by nucleotide affinity-exchange chromatography
    • Volont́e, C. and Greene, L. A. (1992) Nerve growth factor-Activated protein kinase N. Characterization and rapid near homogeneity purification by nucleotide affinity-exchange chromatography. J. Biol. Chem. 267, 21663-21670.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21663-21670
    • Volont́e, C.1    Greene, L.A.2
  • 109
    • 0027412317 scopus 로고
    • Association of a purine-Analogue-sensitive protein kinase activity with p75 nerve growth factor receptors
    • Volont́e, C., Ross, A. H. and Greene, L. A. (1993) Association of a purine-Analogue-sensitive protein kinase activity with p75 nerve growth factor receptors. Mol. Biol. Cell 4, 71-78.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 71-78
    • Volont́e, C.1    Ross, A.H.2    Greene, L.A.3
  • 110
    • 0027179060 scopus 로고
    • A purine analog-sensitive protein kinase activity associates with trk nerve growth factor receptors
    • Volont́e, C., Loeb, D. M. and Greene, L. A. (1993) A purine analog-sensitive protein kinase activity associates with Trk nerve growth factor receptors. J. Neurochem. 61, 664-672.
    • (1993) J. Neurochem , vol.61 , pp. 664-672
    • Volont́e, C.1    Loeb, D.M.2    Greene, L.A.3
  • 111
    • 0024425111 scopus 로고
    • Differential inhibition of nerve growth factor responses by purine analogues: Correlation with inhibition of a nerve growth factor-Activated protein kinase
    • Volont́e, C., Rukenstein, A., Loeb, D. M. and Greene, L. A. (1989) Differential inhibition of nerve growth factor responses by purine analogues: correlation with inhibition of a nerve growth factor-Activated protein kinase. J. Cell Biol. 109, 2395-2403.
    • (1989) J. Cell Biol , vol.109 , pp. 2395-2403
    • Volont́e, C.1    Rukenstein, A.2    Loeb, D.M.3    Greene, L.A.4
  • 112
    • 0025353246 scopus 로고
    • Induction of ornithine decarboxylase by nerve growth factor in pc12 cells: Dissection by purine analogues
    • Volont́e, C. and Greene, L. A. (1990) Induction of ornithine decarboxylase by nerve growth factor in PC12 cells: dissection by purine analogues. J. Biol. Chem. 265, 11050-11055.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11050-11055
    • Volont́e, C.1    Greene, L.A.2
  • 113
    • 0025381729 scopus 로고
    • Multiple pathways of n-kinase activation in pc12 cells
    • Rowland-Gagńe, E. and Greene, L. A. (1990) Multiple pathways of N-kinase activation in PC12 cells. J. Neurochem. 54, 423-433.
    • (1990) J. Neurochem , vol.54 , pp. 423-433
    • Rowland-Gagńe, E.1    Greene, L.A.2
  • 114
    • 33845335809 scopus 로고    scopus 로고
    • Mst3b, a purine-sensitive ste20-like protein kinase, regulates axon outgrowth
    • Irwin, N., Li, Y.-M., O'Toole, J. E. and Benowitz, L. I. (2006) Mst3b, a purine-sensitive Ste20-like protein kinase, regulates axon outgrowth. Proc. Natl. Acad. Sci. U.S.A. 103, 18320-18325.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18320-18325
    • Irwin, N.1    Li, Y.-M.2    O'Toole, J.E.3    Benowitz, L.I.4
  • 115
    • 71149108631 scopus 로고    scopus 로고
    • Mst3b, an ste20-like kinase, regulates axon regeneration in mature cns and pns pathways
    • Lorber, B., Howe, M. L., Benowitz, L. I. and Irwin, N. (2009) Mst3b, an Ste20-like kinase, regulates axon regeneration in mature CNS and PNS pathways. Nat. Neurosci. 12, 1407-1414.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1407-1414
    • Lorber, B.1    Howe, M.L.2    Benowitz, L.I.3    Irwin, N.4
  • 117
    • 0034332067 scopus 로고    scopus 로고
    • A purine-sensitive pathway regulates multiple genes involved in axon regeneration in goldfish retinal ganglion cells
    • Petrausch, B., Tabibiazar, R., Roser, T., Jing, Y., Goldman, D., Stuermer, C. A. O., Irwin, N. and Benowitz, L. I. (2000) A purine-sensitive pathway regulates multiple genes involved in axon regeneration in goldfish retinal ganglion cells. J. Neurosci. 20, 8031-8041.
    • (2000) J. Neurosci , vol.20 , pp. 8031-8041
    • Petrausch, B.1    Tabibiazar, R.2    Roser, T.3    Jing, Y.4    Goldman, D.5    Stuermer, C.A.O.6    Irwin, N.7    Benowitz, L.I.8
  • 119
    • 84862234338 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray analysis of the c-terminal domain of ccm2, part of a novel adaptor protein involved in cerebral cavernous malformations
    • Wang, X., Ding, J. and Wang, D. (2012) Crystallization and preliminary X-ray analysis of the C-terminal domain of CCM2, part of a novel adaptor protein involved in cerebral cavernous malformations. Acta Crystallogr., Sect. F: Struct. Biol. Crystal. Commun. 68, 683-686.
    • (2012) Acta Crystallogr., Sect. F: Struct. Biol. Crystal. Commun , vol.68 , pp. 683-686
    • Wang, X.1    Ding, J.2    Wang, D.3
  • 124
    • 38649127572 scopus 로고    scopus 로고
    • Mammalian ste20-like protein kinase 3 mediates trophoblast apoptosis in spontaneous delivery
    • Wu, H.-Y., Lin, C.-Y., Lin, T.-Y., Chen, T.-C. and Yuan, C.-J. (2008) Mammalian Ste20-like protein kinase 3 mediates trophoblast apoptosis in spontaneous delivery. Apoptosis 13, 283-294.
    • (2008) Apoptosis , vol.13 , pp. 283-294
    • Wu, H.-Y.1    Lin, C.-Y.2    Lin, T.-Y.3    Chen, T.-C.4    Yuan, C.-J.5
  • 125
    • 70549091183 scopus 로고    scopus 로고
    • Mammalian ste20-like protein kinase 3 induces a caspase-independent apoptotic pathway
    • Lin, C.-Y., Wu, H.-Y., Wang, P.-L. and Yuan, C.-J. (2010) Mammalian Ste20-like protein kinase 3 induces a caspase-independent apoptotic pathway. Int. J. Biochem. Cell Biol. 42, 98-105.
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , pp. 98-105
    • Lin, C.-Y.1    Wu, H.-Y.2    Wang, P.-L.3    Yuan, C.-J.4
  • 126
    • 78650516076 scopus 로고    scopus 로고
    • Post-translational myristoylation: Fat matters in cellular life and death
    • Martin, D. D. O., Beauchamp, E. and Berthiaume, L. G. (2011) Post-translational myristoylation: fat matters in cellular life and death. Biochimie 93, 18-31.
    • (2011) Biochimie , vol.93 , pp. 18-31
    • Martin, D.D.O.1    Beauchamp, E.2    Berthiaume, L.G.3
  • 127
    • 40449086667 scopus 로고    scopus 로고
    • Rapid detection, discovery, and identification of post-translationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog
    • Martin, D. D. O., Vilas, G. L., Prescher, J. A., Rajaiah, G., Falck, J. R., Bertozzi, C. R. and Berthiaume, L. G. (2008) Rapid detection, discovery, and identification of post-translationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog. FASEB J. 22, 797-806.
    • (2008) FASEB J. , vol.22 , pp. 797-806
    • Martin, D.D.O.1    Vilas, G.L.2    Prescher, J.A.3    Rajaiah, G.4    Falck, J.R.5    Bertozzi, C.R.6    Berthiaume, L.G.7
  • 130
    • 28544435761 scopus 로고    scopus 로고
    • Regulation of ndr protein kinase by hydrophobic motif phosphorylation mediated by the mammalian ste20-like kinase mst3
    • Stegert, M. R., Hergovich, A., Tamaskovic, R., Bichsel, S. J. and Hemmings, B. A. (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
  • 131
    • 2542482742 scopus 로고    scopus 로고
    • Regulation of ndr2 protein kinase by multi-site phosphorylation and the s100b calcium-binding protein
    • Stegert, M. R., Tamaskovic, R., Bichsel, S. J., Hergovich, A. and Hemmings, B. A. (2004) Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein. J. Biol. Chem. 279, 23806-23812.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23806-23812
    • Stegert, M.R.1    Tamaskovic, R.2    Bichsel, S.J.3    Hergovich, A.4    Hemmings, B.A.5
  • 132
    • 2642546543 scopus 로고    scopus 로고
    • Human mob proteins regulate the ndr1 and ndr2 serine-threonine kinases
    • Devroe, E., Erdjument-Bromage, H., Tempst, P. and Silver, P. A. (2004) Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases. J. Biol. Chem. 279, 24444-24451.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24444-24451
    • Devroe, E.1    Erdjument-Bromage, H.2    Tempst, P.3    Silver, P.A.4
  • 133
    • 45449102823 scopus 로고    scopus 로고
    • Nuclear dbf2-related protein kinases (ndrs) in isolated cardiac myocytes and the myocardium: Activation by cellular stresses and by phosphoprotein serine-/threonine phosphatase inhibitors
    • Fuller, S. J., Pikkarainen, S., Tham, E. L., Cullingford, T. E., Molkentin, J. D., Cornils, H., Hergovich, A., Hemmings, B. A., Clerk, A. and Sugden, P. H. (2008) Nuclear Dbf2-related protein kinases (NDRs) in isolated cardiac myocytes and the myocardium: Activation by cellular stresses and by phosphoprotein serine-/threonine phosphatase inhibitors. Cell. Signalling 20, 1564-1577.
    • (2008) Cell. Signalling , vol.20 , pp. 1564-1577
    • Fuller, S.J.1    Pikkarainen, S.2    Tham, E.L.3    Cullingford, T.E.4    Molkentin, J.D.5    Cornils, H.6    Hergovich, A.7    Hemmings, B.A.8    Clerk, A.9    Sugden, P.H.10
  • 134
    • 33847080309 scopus 로고    scopus 로고
    • Centrosome-Associated ndr kinase regulates centrosome duplication
    • Hergovich, A., Lamla, S., Nigg, E. A. and Hemmings, B. A. (2007) Centrosome-Associated NDR kinase regulates centrosome duplication. Mol. Cell 25, 625-634.
    • (2007) Mol. Cell , vol.25 , pp. 625-634
    • Hergovich, A.1    Lamla, S.2    Nigg, E.A.3    Hemmings, B.A.4
  • 135
    • 79953799132 scopus 로고    scopus 로고
    • Human ndr kinases control g1/s cell cycle transition by directly regulating p21 stability
    • Cornils, H., Kohler, R. S., Hergovich, A. and Hemmings, B. A. (2011) Human NDR kinases control G1/S cell cycle transition by directly regulating p21 stability. Mol. Cell. Biol. 31, 1382-1395.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1382-1395
    • Cornils, H.1    Kohler, R.S.2    Hergovich, A.3    Hemmings, B.A.4
  • 140
    • 9444226945 scopus 로고    scopus 로고
    • Molecular delineation of deletions on 2q37.3 in three cases with an albright hereditary osteodystrophy-like phenotype
    • Shrimpton, A. E., Braddock, B. R., Thomson, L. L., Stein, C. K. and Hoo, J. J. (2004) Molecular delineation of deletions on 2q37.3 in three cases with an Albright hereditary osteodystrophy-like phenotype. Clin. Genet. 66, 537-544.
    • (2004) Clin. Genet. , vol.66 , pp. 537-544
    • Shrimpton, A.E.1    Braddock, B.R.2    Thomson, L.L.3    Stein, C.K.4    Hoo, J.J.5
  • 142
    • 58849139151 scopus 로고    scopus 로고
    • Farp2 and stk25 are candidate genes for the hdl cholesterol locus on mouse chromosome 1
    • Su, Z., Cox, A., Shen, Y., Stylianou, I. M. and Paigen, B. (2009) Farp2 and Stk25 are candidate genes for the HDL cholesterol locus on mouse chromosome 1. Arterioscler. Thromb. Vasc. Biol. 29, 107-113.
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 107-113
    • Su, Z.1    Cox, A.2    Shen, Y.3    Stylianou, I.M.4    Paigen, B.5
  • 144
    • 84865407400 scopus 로고    scopus 로고
    • Serine/threonine protein kinase 25 (stk25): A novel negative regulator of lipid and glucose metabolism in rodent and human skeletal muscle
    • Nerstedt, A., Cansby, E., Andersson, C. X., Laakso, M., Staňćakov́a, A., Bl̈uher, M., Smith, U. and Mahlapuu, M. (2012) Serine/threonine protein kinase 25 (STK25): A novel negative regulator of lipid and glucose metabolism in rodent and human skeletal muscle. Diabetologia 55, 1797-1807.
    • (2012) Diabetologia , vol.55 , pp. 1797-1807
    • Nerstedt, A.1    Cansby, E.2    Andersson, C.X.3    Laakso, M.4    Staňć akov́a, A.5    Bl̈uher, M.6    Smith, U.7    Mahlapuu, M.8
  • 145
    • 77958581183 scopus 로고    scopus 로고
    • Mammalian sterile 20-like kinase 3 (mst3) mediates oxidative stress-induced cell death by modulation jnk activation
    • Chen, C. B., Ng, J. K., Choo, P. H., Wu, W. and Porter, A. G. (2009) Mammalian sterile 20-like kinase 3 (MST3) mediates oxidative stress-induced cell death by modulation JNK activation. Biosci. Rep. 29, 405-415.
    • (2009) Biosci. Rep. , vol.29 , pp. 405-415
    • Chen, C.B.1    Ng, J.K.2    Choo, P.H.3    Wu, W.4    Porter, A.G.5
  • 146
    • 79959564695 scopus 로고    scopus 로고
    • The intfold server: An integrated web resource for protein fold recognition, 3d model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction
    • Roche, D. B., Buenavista, M. T., Tetchner, S. J. and McGuffin, L. J. (2011) The IntFOLD server: An integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction. Nucleic Acids Res. 39, W171-W176.
    • (2011) Nucleic Acids Res , vol.39
    • Roche, D.B.1    Buenavista, M.T.2    Tetchner, S.J.3    McGuffin, L.J.4
  • 147
    • 80855123693 scopus 로고    scopus 로고
    • Automated tertiary structure prediction with accurate local model quality assessment using the intfold-ts method
    • McGuffin, L. J. and Roche, D. B. (2011) Automated tertiary structure prediction with accurate local model quality assessment using the IntFOLD-TS method. Proteins 79 (Suppl. 10), 137-146.
    • (2011) Proteins , vol.79 , Issue.SUPPL. 10 , pp. 137-146
    • McGuffin, L.J.1    Roche, D.B.2
  • 148
    • 84864125649 scopus 로고    scopus 로고
    • Improvement of 3d protein models using multiple templates guided by single-template model quality assessment
    • Buenavista, M. T., Roche, D. B. and McGuffin, L. J. (2012) Improvement of 3D protein models using multiple templates guided by single-template model quality assessment. Bioinformatics 28, 1851-1857.
    • (2012) Bioinformatics , vol.28 , pp. 1851-1857
    • Buenavista, M.T.1    Roche, D.B.2    McGuffin, L.J.3
  • 149
    • 49549111841 scopus 로고    scopus 로고
    • Intrinsic disorder prediction from the analysis of multiple protein fold recognition models
    • McGuffin, L. J. (2008) Intrinsic disorder prediction from the analysis of multiple protein fold recognition models. Bioinformatics 24, 1798-1804.
    • (2008) Bioinformatics , vol.24 , pp. 1798-1804
    • McGuffin, L.J.1
  • 150
    • 77950478720 scopus 로고    scopus 로고
    • Rapid model quality assessment for protein structure predictions using the comparison of multiple models without structural alignments
    • McGuffin, L. J. and Roche, D. B. (2010) Rapid model quality assessment for protein structure predictions using the comparison of multiple models without structural alignments. Bioinformatics 26, 182-188.
    • (2010) Bioinformatics , vol.26 , pp. 182-188
    • McGuffin, L.J.1    Roche, D.B.2
  • 151
    • 0028102478 scopus 로고
    • Cleavage of poly(adp-ribose) polymerase by a proteinase with properties like ice
    • Lazebnik, Y. A., Kaufmann, S. H., Desnoyers, S., Poirier, G. G. and Earnshaw, W. C. (1994) Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371, 346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.