메뉴 건너뛰기




Volumn 358, Issue 3, 2007, Pages 783-788

Human NIMA-related kinase 6 is one of the Fe65 WW domain binding proteins

Author keywords

Apoptosis; Cell cycle; Fe65; Nek6; Protein protein interaction; Signal transduction; Subcellular localization; WW domain

Indexed keywords

MUTANT PROTEIN; NEVER IN MITOSIS GENE A; PROTEIN FE65; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 34249338711     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.04.203     Document Type: Article
Times cited : (11)

References (25)
  • 1
    • 29244456404 scopus 로고    scopus 로고
    • Caught Nek-ing: cilia and centrioles
    • Quarmby L.M., and Mahjoub M.R. Caught Nek-ing: cilia and centrioles. J. Cell Sci. 118 (2005) 5161-5169
    • (2005) J. Cell Sci. , vol.118 , pp. 5161-5169
    • Quarmby, L.M.1    Mahjoub, M.R.2
  • 3
    • 0034283237 scopus 로고    scopus 로고
    • Isolation and characterization of two evolutionarily conserved murine kinases (Nek6 and nek7) related to the fungal mitotic regulator, NIMA
    • Kandli M., Feige E., Chen A., Kilfin G., and Motro B. Isolation and characterization of two evolutionarily conserved murine kinases (Nek6 and nek7) related to the fungal mitotic regulator, NIMA. Genomics 68 (2000) 187-196
    • (2000) Genomics , vol.68 , pp. 187-196
    • Kandli, M.1    Feige, E.2    Chen, A.3    Kilfin, G.4    Motro, B.5
  • 4
    • 0035822699 scopus 로고    scopus 로고
    • Identification of the NIMA family kinases NEK6/7 as regulators of the p70 ribosomal S6 kinase
    • Belham C., Comb M.J., and Avruch J. Identification of the NIMA family kinases NEK6/7 as regulators of the p70 ribosomal S6 kinase. Curr. Biol. 11 (2001) 1155-1167
    • (2001) Curr. Biol. , vol.11 , pp. 1155-1167
    • Belham, C.1    Comb, M.J.2    Avruch, J.3
  • 5
    • 0036290004 scopus 로고    scopus 로고
    • Identification and characterization of Nek6 protein kinase, a potential human homolog of NIMA histone H3 kinase
    • Hashimoto Y., Akita H., Hibino M., Kohri K., and Nakanishi M. Identification and characterization of Nek6 protein kinase, a potential human homolog of NIMA histone H3 kinase. Biochem. Biophys. Res. Commun. 293 (2002) 753-758
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 753-758
    • Hashimoto, Y.1    Akita, H.2    Hibino, M.3    Kohri, K.4    Nakanishi, M.5
  • 6
    • 0036645394 scopus 로고    scopus 로고
    • Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression
    • Roig J., Mikhailov A., Belham C., and Avruch J. Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression. Genes Dev. 16 (2002) 1640-1658
    • (2002) Genes Dev. , vol.16 , pp. 1640-1658
    • Roig, J.1    Mikhailov, A.2    Belham, C.3    Avruch, J.4
  • 7
    • 0037008773 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of NIMA-related kinase-6 (NEK6). Evidence that NEK6 does not phosphorylate the hydrophobic motif of ribosomal S6 protein kinase and serum- and glucocorticoid-induced protein kinase in vivo
    • Lizcano J.M., Deak M., Morrice N., Kieloch A., Hastie C.J., Dong L., Schutkowski M., Reimer U., and Alessi D.R. Molecular basis for the substrate specificity of NIMA-related kinase-6 (NEK6). Evidence that NEK6 does not phosphorylate the hydrophobic motif of ribosomal S6 protein kinase and serum- and glucocorticoid-induced protein kinase in vivo. J. Biol. Chem. 277 (2002) 27839-27849
    • (2002) J. Biol. Chem. , vol.277 , pp. 27839-27849
    • Lizcano, J.M.1    Deak, M.2    Morrice, N.3    Kieloch, A.4    Hastie, C.J.5    Dong, L.6    Schutkowski, M.7    Reimer, U.8    Alessi, D.R.9
  • 8
    • 0042317229 scopus 로고    scopus 로고
    • A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases
    • Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M., and Avruch J. A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases. J. Biol. Chem. 278 (2003) 34897-34909
    • (2003) J. Biol. Chem. , vol.278 , pp. 34897-34909
    • Belham, C.1    Roig, J.2    Caldwell, J.A.3    Aoyama, Y.4    Kemp, B.E.5    Comb, M.6    Avruch, J.7
  • 9
    • 0037459041 scopus 로고    scopus 로고
    • Differential control of the NIMA- related kinases, Nek6 and Nek7, by serum stimulation
    • Minoguchi S., Minoguchi M., and Yoshimura A. Differential control of the NIMA- related kinases, Nek6 and Nek7, by serum stimulation. Biochem. Biophys. Res. Commun. 301 (2003) 899-906
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 899-906
    • Minoguchi, S.1    Minoguchi, M.2    Yoshimura, A.3
  • 10
    • 0347993081 scopus 로고    scopus 로고
    • The serine/threonine kinase Nek6 is required for cell cycle progression through mitosis
    • Yin M.J., Shao L., Voehringer D., Smeal T., and Jallal B. The serine/threonine kinase Nek6 is required for cell cycle progression through mitosis. J. Biol. Chem. 278 (2003) 52454-52460
    • (2003) J. Biol. Chem. , vol.278 , pp. 52454-52460
    • Yin, M.J.1    Shao, L.2    Voehringer, D.3    Smeal, T.4    Jallal, B.5
  • 11
    • 0025953048 scopus 로고
    • A rat brain mRNA encoding a transcriptional activator homologous to the DNA binding domain of retroviral integrases
    • Duilio A., Zambrano N., Mogavero A.R., Ammendola R., Cimino F., and Russo T. A rat brain mRNA encoding a transcriptional activator homologous to the DNA binding domain of retroviral integrases. Nucleic Acids Res. 19 (1991) 5269-5274
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5269-5274
    • Duilio, A.1    Zambrano, N.2    Mogavero, A.R.3    Ammendola, R.4    Cimino, F.5    Russo, T.6
  • 12
    • 0031667822 scopus 로고    scopus 로고
    • The Fe65 and X11 families of proteins: proteins that interact with the Alzheimer's disease amyloid precursor protein
    • McLoughlin D.M., Irving N.G., and Miller C.C. The Fe65 and X11 families of proteins: proteins that interact with the Alzheimer's disease amyloid precursor protein. Biochem. Soc. Trans. 26 (1998) 497-500
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 497-500
    • McLoughlin, D.M.1    Irving, N.G.2    Miller, C.C.3
  • 13
    • 0031717925 scopus 로고    scopus 로고
    • Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein
    • Russo T., Faraonio R., Minopoli G., De Candia P., De Renzis S., and Zambrano N. Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein. FEBS Lett. 434 (1998) 1-7
    • (1998) FEBS Lett. , vol.434 , pp. 1-7
    • Russo, T.1    Faraonio, R.2    Minopoli, G.3    De Candia, P.4    De Renzis, S.5    Zambrano, N.6
  • 14
    • 33646732989 scopus 로고    scopus 로고
    • Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD
    • Nakaya T., and Suzuki T. Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD. Genes Cells. 11 (2006) 633-645
    • (2006) Genes Cells. , vol.11 , pp. 633-645
    • Nakaya, T.1    Suzuki, T.2
  • 15
    • 0029598484 scopus 로고
    • The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphor-tyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein
    • Fiore F., Zambrano N., Minopoli G., Donini V., Duilio A., and Russo T. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphor-tyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein. J. Biol. Chem. 270 (1995) 30853-30856
    • (1995) J. Biol. Chem. , vol.270 , pp. 30853-30856
    • Fiore, F.1    Zambrano, N.2    Minopoli, G.3    Donini, V.4    Duilio, A.5    Russo, T.6
  • 16
    • 0029099161 scopus 로고
    • The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules
    • Chen H.I., and Sudol M. The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc. Natl. Acad. Sci. USA 92 (1995) 7819-7823
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7819-7823
    • Chen, H.I.1    Sudol, M.2
  • 17
    • 0032493814 scopus 로고    scopus 로고
    • The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1
    • Zambrano N., Minopoli G., de Candia P., and Russo T. The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1. J. Biol. Chem. 273 (1998) 20128-20133
    • (1998) J. Biol. Chem. , vol.273 , pp. 20128-20133
    • Zambrano, N.1    Minopoli, G.2    de Candia, P.3    Russo, T.4
  • 18
    • 0345743462 scopus 로고    scopus 로고
    • Adaptor protein interactions: modulators of amyloid precursor protein metabolism and Alzheimer's disease risk?
    • King G.D., and Scott Turner R. Adaptor protein interactions: modulators of amyloid precursor protein metabolism and Alzheimer's disease risk?. Exp. Neurol. 185 (2004) 208-219
    • (2004) Exp. Neurol. , vol.185 , pp. 208-219
    • King, G.D.1    Scott Turner, R.2
  • 20
    • 0032519711 scopus 로고    scopus 로고
    • Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein
    • Duilio A., Faraonio R., Minopoli G., Zambrano N., and Russo T. Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. Biochem J. 330 (1998) 513-519
    • (1998) Biochem J. , vol.330 , pp. 513-519
    • Duilio, A.1    Faraonio, R.2    Minopoli, G.3    Zambrano, N.4    Russo, T.5
  • 21
    • 0036844981 scopus 로고    scopus 로고
    • Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domains
    • Tanahashi T., and Tabira T. Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domains. Biochem. J. 367 (2002) 687-895
    • (2002) Biochem. J. , vol.367 , pp. 687-895
    • Tanahashi, T.1    Tabira, T.2
  • 22
    • 0032223777 scopus 로고    scopus 로고
    • Proteins implicated in Alzheimer disease. The role of FE65, a new adapter which binds to beta-amyloid precursor protein
    • Ermekova K.S., Chang A., Zambrano N., de Candia P., Russo T., and Sudol M. Proteins implicated in Alzheimer disease. The role of FE65, a new adapter which binds to beta-amyloid precursor protein. Adv. Exp. Med. Biol. 446 (1998) 161-180
    • (1998) Adv. Exp. Med. Biol. , vol.446 , pp. 161-180
    • Ermekova, K.S.1    Chang, A.2    Zambrano, N.3    de Candia, P.4    Russo, T.5    Sudol, M.6
  • 23
    • 0031451149 scopus 로고    scopus 로고
    • The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled
    • Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T., and Sudol M. The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. J. Biol. Chem. 272 (1997) 32869-32877
    • (1997) J. Biol. Chem. , vol.272 , pp. 32869-32877
    • Ermekova, K.S.1    Zambrano, N.2    Linn, H.3    Minopoli, G.4    Gertler, F.5    Russo, T.6    Sudol, M.7
  • 24
    • 0035895599 scopus 로고    scopus 로고
    • Functions of WW domains in the nucleus
    • Sudol M., Sliwa K., and Russo T. Functions of WW domains in the nucleus. FEBS Lett. 490 (2001) 190-195
    • (2001) FEBS Lett. , vol.490 , pp. 190-195
    • Sudol, M.1    Sliwa, K.2    Russo, T.3
  • 25
    • 0033546329 scopus 로고    scopus 로고
    • A single point mutation in a group I WW domain shifts its specificity to that of group II WW domains
    • Espanel X., and Sudol M. A single point mutation in a group I WW domain shifts its specificity to that of group II WW domains. J. Biol. Chem. 274 (1999) 17284-17289
    • (1999) J. Biol. Chem. , vol.274 , pp. 17284-17289
    • Espanel, X.1    Sudol, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.