Comparative studies of a new subfamily of human Ste20-like kinases: Homodimerization, subcellular localization, and selective activation of MKK3 and p38

J.T. Yustein, L. Xia, J.M. Kahlenburg, D. Robinson, D. Templeton, H.-J. Kung

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The Sterile-20 or Ste20 family of serine/threonine kinases is a group of signaling molecules whose physiological roles within mammalian cells are just starting to be elucidated. Here, in this report we present the characterization of three human Ste20-like kinases with greater than 90% similarity within their catalytic domains that define a novel subfamily of Ste20s. Members of this kinase family include rat thousand and one (TAO1) and chicken KFC (kinase from chicken). For the lack of a consensus nomenclature in the literature, in this report, we shall call this family hKFC (for their homology to chicken KFC) and the three members hKFC-A, hKFC-B, and hKFC-C, respectively. These kinases have many similarities including an aminoterminal kinase domain, a serine-rich region, and a coiled-coil configuration within the C-terminus. All three kinases are able to activate the p38 MAP kinase pathway through the specific activation of the upstream MKK3 kinase. We also offer evidence, both theoretical and biochemical, showing that these kinases can undergo self-association. Despite these similarities, these kinases differ in tissue distribution, apparent subcellular localization, and feature structural differences largely within the carboxyl-terminal sequence.
Original languageEnglish
Pages (from-to)6129-6141
Number of pages13
JournalOncogene
Volume22
Issue number40
DOIs
Publication statusPublished - 2003
Externally publishedYes

Fingerprint

Phosphotransferases
Chickens
MAP Kinase Signaling System
Protein-Serine-Threonine Kinases
p38 Mitogen-Activated Protein Kinases
Tissue Distribution
Terminology
Serine
Catalytic Domain
Consensus

Keywords

  • p38 MAPK
  • Ste20 kinase
  • TAO
  • mitogen activated protein kinase
  • protein serine threonine kinase
  • sterile 20 kinase
  • unclassified drug
  • amino terminal sequence
  • article
  • carboxy terminal sequence
  • cellular distribution
  • controlled study
  • dimerization
  • enzyme activation
  • enzyme phosphorylation
  • human
  • human cell
  • nonhuman
  • nucleotide sequence
  • priority journal
  • protein domain
  • protein family
  • sequence homology
  • signal transduction
  • tissue distribution
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cercopithecus aethiops
  • COS Cells
  • Dimerization
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Isoenzymes
  • Jurkat Cells
  • Male
  • MAP Kinase Kinase 3
  • Mitogen-Activated Protein Kinase Kinases
  • Mitogen-Activated Protein Kinases
  • Molecular Sequence Data
  • p38 Mitogen-Activated Protein Kinases
  • Phylogeny
  • Protein Conformation
  • Protein-Serine-Threonine Kinases
  • Protein-Tyrosine Kinases
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
  • Subcellular Fractions
  • Tissue Distribution
  • Gallus gallus
  • Mammalia

Cite this

Comparative studies of a new subfamily of human Ste20-like kinases: Homodimerization, subcellular localization, and selective activation of MKK3 and p38. / Yustein, J.T.; Xia, L.; Kahlenburg, J.M.; Robinson, D.; Templeton, D.; Kung, H.-J.

In: Oncogene, Vol. 22, No. 40, 2003, p. 6129-6141.

Research output: Contribution to journalArticle

Yustein, J.T. ; Xia, L. ; Kahlenburg, J.M. ; Robinson, D. ; Templeton, D. ; Kung, H.-J. / Comparative studies of a new subfamily of human Ste20-like kinases: Homodimerization, subcellular localization, and selective activation of MKK3 and p38. In: Oncogene. 2003 ; Vol. 22, No. 40. pp. 6129-6141.
@article{8d9452ad1d0e4f41b26ad7f2b620f883,
title = "Comparative studies of a new subfamily of human Ste20-like kinases: Homodimerization, subcellular localization, and selective activation of MKK3 and p38",
abstract = "The Sterile-20 or Ste20 family of serine/threonine kinases is a group of signaling molecules whose physiological roles within mammalian cells are just starting to be elucidated. Here, in this report we present the characterization of three human Ste20-like kinases with greater than 90{\%} similarity within their catalytic domains that define a novel subfamily of Ste20s. Members of this kinase family include rat thousand and one (TAO1) and chicken KFC (kinase from chicken). For the lack of a consensus nomenclature in the literature, in this report, we shall call this family hKFC (for their homology to chicken KFC) and the three members hKFC-A, hKFC-B, and hKFC-C, respectively. These kinases have many similarities including an aminoterminal kinase domain, a serine-rich region, and a coiled-coil configuration within the C-terminus. All three kinases are able to activate the p38 MAP kinase pathway through the specific activation of the upstream MKK3 kinase. We also offer evidence, both theoretical and biochemical, showing that these kinases can undergo self-association. Despite these similarities, these kinases differ in tissue distribution, apparent subcellular localization, and feature structural differences largely within the carboxyl-terminal sequence.",
keywords = "p38 MAPK, Ste20 kinase, TAO, mitogen activated protein kinase, protein serine threonine kinase, sterile 20 kinase, unclassified drug, amino terminal sequence, article, carboxy terminal sequence, cellular distribution, controlled study, dimerization, enzyme activation, enzyme phosphorylation, human, human cell, nonhuman, nucleotide sequence, priority journal, protein domain, protein family, sequence homology, signal transduction, tissue distribution, Amino Acid Sequence, Animals, Cell Line, Cercopithecus aethiops, COS Cells, Dimerization, Gene Expression Regulation, Enzymologic, Humans, Isoenzymes, Jurkat Cells, Male, MAP Kinase Kinase 3, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinases, Molecular Sequence Data, p38 Mitogen-Activated Protein Kinases, Phylogeny, Protein Conformation, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Subcellular Fractions, Tissue Distribution, Gallus gallus, Mammalia",
author = "J.T. Yustein and L. Xia and J.M. Kahlenburg and D. Robinson and D. Templeton and H.-J. Kung",
note = "引用次數:25 Export Date: 9 March 2018 CODEN: ONCNE 通訊地址: Kung, H.-J.; University of California, Davis Cancer Center, UCDMC, Res. III, 4645 2nd Avenue, Sacramento, CA 95817, United States; 電子郵件: hkung@ucdavis.edu 分析序列編號: GENBANK: AAD39480, AF263311, AF263312, AF263313; 化學物質/CAS: mitogen activated protein kinase, 142243-02-5; Isoenzymes; MAP Kinase Kinase 3, EC 2.7.1.-; MAP2K3 protein, human, EC 2.7.1.-; MAP4K4 protein, human, EC 2.7.1.-; Mitogen-Activated Protein Kinase Kinases, EC 2.7.1.-; Mitogen-Activated Protein Kinases, EC 2.7.1.37; p38 Mitogen-Activated Protein Kinases, EC 2.7.1.37; Protein-Serine-Threonine Kinases, EC 2.7.1.37; Protein-Tyrosine Kinases, EC 2.7.1.112; Saccharomyces cerevisiae Proteins; STE20 protein, S cerevisiae, EC 2.7.1.37 參考文獻: Assefa, Z., Garmyn, M., Bouillon, R., Merlevede, W., Vandenheede, J.R., Agonstinis, P., (1997) J. Invest. Dermatol., 108, pp. 886-891; Becker, E., Huynh-Do, U., Holland, S., Pawson, T., Daniel, T.O., Skolnick, E.Y., (2000) Mol. Cell. Biol., 20, pp. 1537-1545; Bost, F., McKay, R., Bost, M., Potapova, O., Dean, N.M., Mercola, D., (1999) Mol. Cell. Biol., 19, pp. 1938-1949; Boulton, T.G., Nye, S.H., Robbins, D.J., Ip, N.Y., Radziejewska, E., Morgenbesser, S.D., DePinho, R.A., Yancopoulos, G.D., (1991) Cell, 65, pp. 663-675; Brown, J.L., Stowers, L., Baer, M., Trejo, J., Coughlin, S., Chant, J., (1996) Curr. Biol., 6, pp. 598-605; Charest, D.L., Mordret, G., Harder, K.W., Jirik, F., Pelech, S.L., (1993) Mol. Cell. Biol., 13, pp. 4679-4690; Chen, Z., Hutchison, M., Cobb, M.H., (1999) J. Biol. Chem., 274, pp. 28803-28807; Chung, C.Y., Firtel, R.A., (1999) J. Cell Biol., 147, pp. 559-576; Creasy, C.L., Chernoff, J., (1995) Gene, 167, pp. 303-306; Creasy, C.L., Chernoff, J., (1995) J. Biol. Chem., 270, pp. 21695-21700; Dan, I., Watanabe, N.M., Kobayashi, T., Yamashita-Suzuki, K., Fukagaya, Y., Kajikawa, E., Kimura, W.K., Kusumi, A., (2000) FEBS Lett., 469, pp. 19-23; Dan, I., Watanabe, N.M., Kusumi, A., (2001) Trends Cell Biol., 11, pp. 220-230; Eby, J.J., Holly, S.P., Van Drogen, F., Grishin, A.V., Peter, M., Drubin, D.G., Blumer, K.J., (1998) Curr. Biol., 8, pp. 967-970; Endo, J., Toyama-Sorimachi, N., Taya, C., Kuramochi-Miyagawa, S., Nagata, K., Kuida, K., Takashi, T., Karasuyama, H., (2000) FEBS Lett., 468, pp. 234-238; Enslen, H., Brancho, D.M., Davis, R.J., (2000) EMBO J., 19, pp. 1301-1311; Fanger, G.R., Gerwins, P., Widmann, C., Jarpe, M.B., Johnson, G.L., (1997) Curr. Opin. Genet. Dev., 7, pp. 67-74; Frost, J.A., Xu, S., Hutchison, M.R., Marcus, S., Cobb, M.H., (1996) Mol. Cell. Biol., 16, pp. 3707-3713; Geng, Y., Valbracht, J., Lotz, M., (1996) J. Clin. Invest., 98, pp. 2425-2430; Holly, S.P., Blumer, K.J., (1999) J. Cell Biol., 147, pp. 845-856; Hu, M.C., Qiu, W.R., Wang, X., Meyer, C.F., Tan, T.H., (1996) Genes Dev., 10, pp. 2251-2264; Hutchison, M., Berman, K.S., Cobb, M.H., (1998) J. Biol. Chem., 273, pp. 28625-28632; Ichijo, H., Nishida, E., Irie, K., Ten Dijke, P., Saitoh, M., Moriguchi, T., Takagi, M., Gotoh, Y., (1997) Science, 275, pp. 90-94; Katz, P., Whalen, G., Kerhl, J.H., (1994) J. Biol. Chem., 269, pp. 16802-16809; Kyriakis, J.M., Avruch, J., (1996) Bioessays, 18, pp. 567-577; Ling, P., Meyer, C.F., Redmond, L.P., Shui, J.W., Davis, B., Rich, R.R., Hu, M.C., Tan, T.H., (2001) J. Biol. Chem., 276, pp. 18908-18914; Ling, P., Yao, Z., Meyer, C.F., Wang, X.S., Oehrl, W., Feller, S.M., Tan, T.H., (1999) Mol. Cell. Biol., 19, pp. 1359-1368; Lu, H.T., Yang, D.D., Wysk, M., Gatti, E., Mellman, I., Davis, R.J., Flavell, R.A., (1999) EMBO J., 18, pp. 1845-1857; Lupas, A., Van Dyke, M., Stock, J., (1991) Science, 252, pp. 1162-1164; Manser, E., Leung, T., Salihuddin, H., Zhao, Z.S., Lim, L., (1994) Nature, 367, pp. 40-46; Moore, T.M., Garg, R., Johnson, C., Coptcoat, M.J., Ridley, A.J., Morris, J.D., (2000) J. Biol. Chem., 275, pp. 4311-4322; Moriguchi, T., Kuroyanagi, N., Yamaguchi, K., Gotoh, Y., Irie, K., Kano, T., Shirkabe, K., Hagiwara, M., (1996) J. Biol. Chem., 271, pp. 13675-13679; Oehrl, W., Kardinal, C., Ruf, S., Adermann, K., Groffen, J., Feng, G.S., Blenis, J., Feller, S.M., (1998) Oncogene, 17, pp. 1893-1901; Parrini, M.C., Lei, M., Harrison, S.C., Mayer, B.J., (2002) Mol. Cell, 9, pp. 73-83; Paul, A., Wilson, S., Belham, C.M., Robinson, C.J., Scott, P.H., Gould, G.W., Plevin, R., (1997) Cell Signal, 9, pp. 403-410; Peraldi, P., Scimeca, J.C., Filloux, C., Van Obberghen, E., (1993) Endocrinology, 132, pp. 2578-2585; Pombo, C.M., Kehrl, J.H., Sanchez, I., Katz, P., Avruch, J., Zon, L.I., Woodgett, J.R., Kyriakis, J.M., (1995) Nature, 377, pp. 750-754; Rousseau, S., Houle, F., Landry, J., Huot, J., (1997) Oncogene, 15, pp. 2169-2177; Su, Y.C., Han, J., Xu, S., Cobb, M., Skolnik, E.Y., (1997) EMBO J., 16, pp. 1270-1290; Takekawa, M., Posas, F., Saito, H., (1997) EMBO J., 16, pp. 4973-4982; Tassi, E., Biesova, Z., Di Force, P.P., Gutkind, J.S., Wong, W.T., (1999) J. Biol. Chem., 274, pp. 33287-33295; Tibbles, L.A., Ing, Y.L., Kiefer, F., Chan, J., Iscove, N., Woodgett, J.R., Lassam, N.J., (1996) EMBO J., 15, pp. 7026-7035; Wolf, E., Kim, P.S., Berger, B., (1997) Protein Sci., 6, pp. 1179-1189; Wysk, M., Yang, D.D., Lu, H.T., Flavell, R.A., Davis, R.J., (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 3763-3768; Xing, J., Kornhauser, J.M., Xia, Z., Thiele, E.A., Greenberg, M.E., (1998) Mol. Cell. Biol., 18, pp. 1946-1955; Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T., Tohyama, M., (2001) J. Biol. Chem., 276, pp. 13935-13940; Yustein, J.T., Li, D., Robinson, D., Kung, H.J., (2000) Oncogene, 19, pp. 710-718; Zanke, B.W., Boudreau, K., Rubie, E., Winnett, E., Tibbles, L.A., Zon, L., Kyriakis, J., Woodgett, J.R., (1996) Curr. Biol., 6, pp. 606-613; Zanke, B.W., Rubie, E.A., Winnett, E., Chan, J., Randall, S., Parsons, M., Boudreau, K., Woodgett, J.R., (1996) J. Biol. Chem., 271, pp. 29876-29881; Zhou, G., Lee, S.C., Yao, Z., Tan, T.H., (1999) J. Biol. Chem., 274, pp. 13133-13138",
year = "2003",
doi = "10.1038/sj.onc.1206605",
language = "English",
volume = "22",
pages = "6129--6141",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "40",

}

TY - JOUR

T1 - Comparative studies of a new subfamily of human Ste20-like kinases: Homodimerization, subcellular localization, and selective activation of MKK3 and p38

AU - Yustein, J.T.

AU - Xia, L.

AU - Kahlenburg, J.M.

AU - Robinson, D.

AU - Templeton, D.

AU - Kung, H.-J.

N1 - 引用次數:25 Export Date: 9 March 2018 CODEN: ONCNE 通訊地址: Kung, H.-J.; University of California, Davis Cancer Center, UCDMC, Res. III, 4645 2nd Avenue, Sacramento, CA 95817, United States; 電子郵件: hkung@ucdavis.edu 分析序列編號: GENBANK: AAD39480, AF263311, AF263312, AF263313; 化學物質/CAS: mitogen activated protein kinase, 142243-02-5; Isoenzymes; MAP Kinase Kinase 3, EC 2.7.1.-; MAP2K3 protein, human, EC 2.7.1.-; MAP4K4 protein, human, EC 2.7.1.-; Mitogen-Activated Protein Kinase Kinases, EC 2.7.1.-; Mitogen-Activated Protein Kinases, EC 2.7.1.37; p38 Mitogen-Activated Protein Kinases, EC 2.7.1.37; Protein-Serine-Threonine Kinases, EC 2.7.1.37; Protein-Tyrosine Kinases, EC 2.7.1.112; Saccharomyces cerevisiae Proteins; STE20 protein, S cerevisiae, EC 2.7.1.37 參考文獻: Assefa, Z., Garmyn, M., Bouillon, R., Merlevede, W., Vandenheede, J.R., Agonstinis, P., (1997) J. Invest. Dermatol., 108, pp. 886-891; Becker, E., Huynh-Do, U., Holland, S., Pawson, T., Daniel, T.O., Skolnick, E.Y., (2000) Mol. Cell. Biol., 20, pp. 1537-1545; Bost, F., McKay, R., Bost, M., Potapova, O., Dean, N.M., Mercola, D., (1999) Mol. Cell. Biol., 19, pp. 1938-1949; Boulton, T.G., Nye, S.H., Robbins, D.J., Ip, N.Y., Radziejewska, E., Morgenbesser, S.D., DePinho, R.A., Yancopoulos, G.D., (1991) Cell, 65, pp. 663-675; Brown, J.L., Stowers, L., Baer, M., Trejo, J., Coughlin, S., Chant, J., (1996) Curr. Biol., 6, pp. 598-605; Charest, D.L., Mordret, G., Harder, K.W., Jirik, F., Pelech, S.L., (1993) Mol. Cell. Biol., 13, pp. 4679-4690; Chen, Z., Hutchison, M., Cobb, M.H., (1999) J. Biol. Chem., 274, pp. 28803-28807; Chung, C.Y., Firtel, R.A., (1999) J. Cell Biol., 147, pp. 559-576; Creasy, C.L., Chernoff, J., (1995) Gene, 167, pp. 303-306; Creasy, C.L., Chernoff, J., (1995) J. Biol. Chem., 270, pp. 21695-21700; Dan, I., Watanabe, N.M., Kobayashi, T., Yamashita-Suzuki, K., Fukagaya, Y., Kajikawa, E., Kimura, W.K., Kusumi, A., (2000) FEBS Lett., 469, pp. 19-23; Dan, I., Watanabe, N.M., Kusumi, A., (2001) Trends Cell Biol., 11, pp. 220-230; Eby, J.J., Holly, S.P., Van Drogen, F., Grishin, A.V., Peter, M., Drubin, D.G., Blumer, K.J., (1998) Curr. Biol., 8, pp. 967-970; Endo, J., Toyama-Sorimachi, N., Taya, C., Kuramochi-Miyagawa, S., Nagata, K., Kuida, K., Takashi, T., Karasuyama, H., (2000) FEBS Lett., 468, pp. 234-238; Enslen, H., Brancho, D.M., Davis, R.J., (2000) EMBO J., 19, pp. 1301-1311; Fanger, G.R., Gerwins, P., Widmann, C., Jarpe, M.B., Johnson, G.L., (1997) Curr. Opin. Genet. Dev., 7, pp. 67-74; Frost, J.A., Xu, S., Hutchison, M.R., Marcus, S., Cobb, M.H., (1996) Mol. Cell. Biol., 16, pp. 3707-3713; Geng, Y., Valbracht, J., Lotz, M., (1996) J. Clin. Invest., 98, pp. 2425-2430; Holly, S.P., Blumer, K.J., (1999) J. Cell Biol., 147, pp. 845-856; Hu, M.C., Qiu, W.R., Wang, X., Meyer, C.F., Tan, T.H., (1996) Genes Dev., 10, pp. 2251-2264; Hutchison, M., Berman, K.S., Cobb, M.H., (1998) J. Biol. Chem., 273, pp. 28625-28632; Ichijo, H., Nishida, E., Irie, K., Ten Dijke, P., Saitoh, M., Moriguchi, T., Takagi, M., Gotoh, Y., (1997) Science, 275, pp. 90-94; Katz, P., Whalen, G., Kerhl, J.H., (1994) J. Biol. Chem., 269, pp. 16802-16809; Kyriakis, J.M., Avruch, J., (1996) Bioessays, 18, pp. 567-577; Ling, P., Meyer, C.F., Redmond, L.P., Shui, J.W., Davis, B., Rich, R.R., Hu, M.C., Tan, T.H., (2001) J. Biol. Chem., 276, pp. 18908-18914; Ling, P., Yao, Z., Meyer, C.F., Wang, X.S., Oehrl, W., Feller, S.M., Tan, T.H., (1999) Mol. Cell. Biol., 19, pp. 1359-1368; Lu, H.T., Yang, D.D., Wysk, M., Gatti, E., Mellman, I., Davis, R.J., Flavell, R.A., (1999) EMBO J., 18, pp. 1845-1857; Lupas, A., Van Dyke, M., Stock, J., (1991) Science, 252, pp. 1162-1164; Manser, E., Leung, T., Salihuddin, H., Zhao, Z.S., Lim, L., (1994) Nature, 367, pp. 40-46; Moore, T.M., Garg, R., Johnson, C., Coptcoat, M.J., Ridley, A.J., Morris, J.D., (2000) J. Biol. Chem., 275, pp. 4311-4322; Moriguchi, T., Kuroyanagi, N., Yamaguchi, K., Gotoh, Y., Irie, K., Kano, T., Shirkabe, K., Hagiwara, M., (1996) J. Biol. Chem., 271, pp. 13675-13679; Oehrl, W., Kardinal, C., Ruf, S., Adermann, K., Groffen, J., Feng, G.S., Blenis, J., Feller, S.M., (1998) Oncogene, 17, pp. 1893-1901; Parrini, M.C., Lei, M., Harrison, S.C., Mayer, B.J., (2002) Mol. Cell, 9, pp. 73-83; Paul, A., Wilson, S., Belham, C.M., Robinson, C.J., Scott, P.H., Gould, G.W., Plevin, R., (1997) Cell Signal, 9, pp. 403-410; Peraldi, P., Scimeca, J.C., Filloux, C., Van Obberghen, E., (1993) Endocrinology, 132, pp. 2578-2585; Pombo, C.M., Kehrl, J.H., Sanchez, I., Katz, P., Avruch, J., Zon, L.I., Woodgett, J.R., Kyriakis, J.M., (1995) Nature, 377, pp. 750-754; Rousseau, S., Houle, F., Landry, J., Huot, J., (1997) Oncogene, 15, pp. 2169-2177; Su, Y.C., Han, J., Xu, S., Cobb, M., Skolnik, E.Y., (1997) EMBO J., 16, pp. 1270-1290; Takekawa, M., Posas, F., Saito, H., (1997) EMBO J., 16, pp. 4973-4982; Tassi, E., Biesova, Z., Di Force, P.P., Gutkind, J.S., Wong, W.T., (1999) J. Biol. Chem., 274, pp. 33287-33295; Tibbles, L.A., Ing, Y.L., Kiefer, F., Chan, J., Iscove, N., Woodgett, J.R., Lassam, N.J., (1996) EMBO J., 15, pp. 7026-7035; Wolf, E., Kim, P.S., Berger, B., (1997) Protein Sci., 6, pp. 1179-1189; Wysk, M., Yang, D.D., Lu, H.T., Flavell, R.A., Davis, R.J., (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 3763-3768; Xing, J., Kornhauser, J.M., Xia, Z., Thiele, E.A., Greenberg, M.E., (1998) Mol. Cell. Biol., 18, pp. 1946-1955; Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T., Tohyama, M., (2001) J. Biol. Chem., 276, pp. 13935-13940; Yustein, J.T., Li, D., Robinson, D., Kung, H.J., (2000) Oncogene, 19, pp. 710-718; Zanke, B.W., Boudreau, K., Rubie, E., Winnett, E., Tibbles, L.A., Zon, L., Kyriakis, J., Woodgett, J.R., (1996) Curr. Biol., 6, pp. 606-613; Zanke, B.W., Rubie, E.A., Winnett, E., Chan, J., Randall, S., Parsons, M., Boudreau, K., Woodgett, J.R., (1996) J. Biol. Chem., 271, pp. 29876-29881; Zhou, G., Lee, S.C., Yao, Z., Tan, T.H., (1999) J. Biol. Chem., 274, pp. 13133-13138

PY - 2003

Y1 - 2003

N2 - The Sterile-20 or Ste20 family of serine/threonine kinases is a group of signaling molecules whose physiological roles within mammalian cells are just starting to be elucidated. Here, in this report we present the characterization of three human Ste20-like kinases with greater than 90% similarity within their catalytic domains that define a novel subfamily of Ste20s. Members of this kinase family include rat thousand and one (TAO1) and chicken KFC (kinase from chicken). For the lack of a consensus nomenclature in the literature, in this report, we shall call this family hKFC (for their homology to chicken KFC) and the three members hKFC-A, hKFC-B, and hKFC-C, respectively. These kinases have many similarities including an aminoterminal kinase domain, a serine-rich region, and a coiled-coil configuration within the C-terminus. All three kinases are able to activate the p38 MAP kinase pathway through the specific activation of the upstream MKK3 kinase. We also offer evidence, both theoretical and biochemical, showing that these kinases can undergo self-association. Despite these similarities, these kinases differ in tissue distribution, apparent subcellular localization, and feature structural differences largely within the carboxyl-terminal sequence.

AB - The Sterile-20 or Ste20 family of serine/threonine kinases is a group of signaling molecules whose physiological roles within mammalian cells are just starting to be elucidated. Here, in this report we present the characterization of three human Ste20-like kinases with greater than 90% similarity within their catalytic domains that define a novel subfamily of Ste20s. Members of this kinase family include rat thousand and one (TAO1) and chicken KFC (kinase from chicken). For the lack of a consensus nomenclature in the literature, in this report, we shall call this family hKFC (for their homology to chicken KFC) and the three members hKFC-A, hKFC-B, and hKFC-C, respectively. These kinases have many similarities including an aminoterminal kinase domain, a serine-rich region, and a coiled-coil configuration within the C-terminus. All three kinases are able to activate the p38 MAP kinase pathway through the specific activation of the upstream MKK3 kinase. We also offer evidence, both theoretical and biochemical, showing that these kinases can undergo self-association. Despite these similarities, these kinases differ in tissue distribution, apparent subcellular localization, and feature structural differences largely within the carboxyl-terminal sequence.

KW - p38 MAPK

KW - Ste20 kinase

KW - TAO

KW - mitogen activated protein kinase

KW - protein serine threonine kinase

KW - sterile 20 kinase

KW - unclassified drug

KW - amino terminal sequence

KW - article

KW - carboxy terminal sequence

KW - cellular distribution

KW - controlled study

KW - dimerization

KW - enzyme activation

KW - enzyme phosphorylation

KW - human

KW - human cell

KW - nonhuman

KW - nucleotide sequence

KW - priority journal

KW - protein domain

KW - protein family

KW - sequence homology

KW - signal transduction

KW - tissue distribution

KW - Amino Acid Sequence

KW - Animals

KW - Cell Line

KW - Cercopithecus aethiops

KW - COS Cells

KW - Dimerization

KW - Gene Expression Regulation, Enzymologic

KW - Humans

KW - Isoenzymes

KW - Jurkat Cells

KW - Male

KW - MAP Kinase Kinase 3

KW - Mitogen-Activated Protein Kinase Kinases

KW - Mitogen-Activated Protein Kinases

KW - Molecular Sequence Data

KW - p38 Mitogen-Activated Protein Kinases

KW - Phylogeny

KW - Protein Conformation

KW - Protein-Serine-Threonine Kinases

KW - Protein-Tyrosine Kinases

KW - Saccharomyces cerevisiae Proteins

KW - Sequence Homology, Amino Acid

KW - Subcellular Fractions

KW - Tissue Distribution

KW - Gallus gallus

KW - Mammalia

U2 - 10.1038/sj.onc.1206605

DO - 10.1038/sj.onc.1206605

M3 - Article

VL - 22

SP - 6129

EP - 6141

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 40

ER -