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Volumn 55, Issue 1, 2003, Pages 23-27

FHA domains as phospho-threonine binding modules in cell signaling

Author keywords

Cell cycle; Checkpoint; Chk2; FHA domain; Phospho threonine binding domain; Protein phosphorylation; Rad53

Indexed keywords

BINDING PROTEIN; FORKHEAD ASSOCIATED PROTEIN; PHOSPHOTHREONINE; UNCLASSIFIED DRUG;

EID: 0037256803     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/1521654031000070636     Document Type: Review
Times cited : (48)

References (31)
  • 1
    • 0029360452 scopus 로고
    • The FHA domain: A putative nuclear signalling domain found in protein kinases and transcription factors
    • Hofmann, K., and Bucher, P. (1995) The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors. Trends Biochem. Sci. 20, 347-349.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 347-349
    • Hofmann, K.1    Bucher, P.2
  • 2
    • 0034531364 scopus 로고    scopus 로고
    • The FHA domain mediates phosphoprotein interactions
    • Li, J., Lee, G., Van Doren, S.R., and Walker, J.C. (2000) The FHA domain mediates phosphoprotein interactions. J. Cell Sci. 113, 4143-4149.
    • (2000) J. Cell Sci. , vol.113 , pp. 4143-4149
    • Li, J.1    Lee, G.2    Van Doren, S.R.3    Walker, J.C.4
  • 3
    • 0036070545 scopus 로고    scopus 로고
    • FHA: A signal transduction domain with diverse specificity and function
    • Tsai, M.-D. (2002) FHA: A signal transduction domain with diverse specificity and function. Structure 10, 887-888.
    • (2002) Structure , vol.10 , pp. 887-888
    • Tsai, M.-D.1
  • 5
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA Domain:Phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • Durocher, D., Taylor, I.A., Sarbassova, D., Haire, L.F., Westcott, S.-L., Jackson, S.P., Smerdon, S.J., and Yaffe, M.B. (2000) The molecular basis of FHA Domain:Phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol. Cell 6, 1169-1182.
    • (2000) Mol. Cell , vol.6 , pp. 1169-1182
    • Durocher, D.1    Taylor, I.A.2    Sarbassova, D.3    Haire, L.F.4    Westcott, S.-L.5    Jackson, S.P.6    Smerdon, S.J.7    Yaffe, M.B.8
  • 6
    • 0033544711 scopus 로고    scopus 로고
    • Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53
    • Liao, H., Byeon, I.J., and Tsai, M.D. (1999) Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53. J. Mol. Biol. 294, 1041-1049.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1041-1049
    • Liao, H.1    Byeon, I.J.2    Tsai, M.D.3
  • 7
    • 0035976793 scopus 로고    scopus 로고
    • Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53
    • Yuan, C., Yongkiettrakul, S., Byeon, I.J., Zhou, S., and Tsai, M.D. (2001) Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. J. Mol. Biol. 314, 563-575.
    • (2001) J. Mol. Biol. , vol.314 , pp. 563-575
    • Yuan, C.1    Yongkiettrakul, S.2    Byeon, I.J.3    Zhou, S.4    Tsai, M.D.5
  • 8
    • 0035976751 scopus 로고    scopus 로고
    • Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: Comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes
    • Byeon, I.J., Yongkiettrakul, S., and Tsai, M.D. (2001) Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes. J. Mol. Biol. 314, 577-588.
    • (2001) J. Mol. Biol. , vol.314 , pp. 577-588
    • Byeon, I.J.1    Yongkiettrakul, S.2    Tsai, M.D.3
  • 11
    • 0028075896 scopus 로고
    • Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase
    • Stone, J.M., Collinge, M.A., Smith, R.D., Horn, M.A., and Walker, J.C. (1994) Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science 266, 793-795.
    • (1994) Science , vol.266 , pp. 793-795
    • Stone, J.M.1    Collinge, M.A.2    Smith, R.D.3    Horn, M.A.4    Walker, J.C.5
  • 12
    • 0033529330 scopus 로고    scopus 로고
    • Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain
    • Li, J., Smith, G.P., and Walker, J.C. (1999) Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain. Proc. Natl. Acad. Sci. USA 96, 7821-7826.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7821-7826
    • Li, J.1    Smith, G.P.2    Walker, J.C.3
  • 13
    • 0032504069 scopus 로고    scopus 로고
    • Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
    • Sun, Z., Hsiao, J., Fay, D.S., and Stern, D.F. (1998) Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint. Science 281, 272-274.
    • (1998) Science , vol.281 , pp. 272-274
    • Sun, Z.1    Hsiao, J.2    Fay, D.S.3    Stern, D.F.4
  • 14
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • Durocher, D., Henckel, J., Ferscht, A.R., and Jackson, S.P. (1999) The FHA domain is a modular phosphopeptide recognition motif. Mol. Cell 4, 387-394.
    • (1999) Mol. Cell , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Ferscht, A.R.3    Jackson, S.P.4
  • 15
    • 0036281710 scopus 로고    scopus 로고
    • Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint
    • Schwartz, M.F., Duong, J.K., Sun, Z., Morrow, J.S., Pradhan, D., and Stern, D.F. (2002) Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint. Mol. Cell 9, 1055-1065.
    • (2002) Mol. Cell , vol.9 , pp. 1055-1065
    • Schwartz, M.F.1    Duong, J.K.2    Sun, Z.3    Morrow, J.S.4    Pradhan, D.5    Stern, D.F.6
  • 18
    • 0037205422 scopus 로고    scopus 로고
    • Phosphorylation of threonine 68 promotes oligomerization and autophosphorylation of the Chk2 protein kinase via the forkhead-associated, FHA) domain
    • Ahn, J.-Y., Li, X., Davis, HL., and Canman, C.E. (2002) Phosphorylation of threonine 68 promotes oligomerization and autophosphorylation of the Chk2 protein kinase via the forkhead-associated, FHA) domain. J. Biol. Chem. 277, 19389-19395.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19389-19395
    • Ahn, J.-Y.1    Li, X.2    Davis, H.L.3    Canman, C.E.4
  • 19
    • 0035848819 scopus 로고    scopus 로고
    • The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis
    • Falck, J., Mailand, N., Syljuasen, R.G., Bartek, J., and Lukas, J. (2001) The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis. Nature 410, 842-847.
    • (2001) Nature , vol.410 , pp. 842-847
    • Falck, J.1    Mailand, N.2    Syljuasen, R.G.3    Bartek, J.4    Lukas, J.5
  • 21
    • 0037151028 scopus 로고    scopus 로고
    • Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks
    • Hammet, A., Pike, BL., and Heierhorst, J. (2002) Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks. J. Biol. Chem. 277, 22469-22474.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22469-22474
    • Hammet, A.1    Pike, B.L.2    Heierhorst, J.3
  • 22
    • 0035957965 scopus 로고    scopus 로고
    • Role of the N-terminal forkhead-associated domain in the cell cycle checkpoint function of the Rad53 kinase
    • Pike, B.L., Hammet, A., and Heierhorst, J. (2001) Role of the N-terminal forkhead-associated domain in the cell cycle checkpoint function of the Rad53 kinase. J. Biol. Chem. 276, 14019-14026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14019-14026
    • Pike, B.L.1    Hammet, A.2    Heierhorst, J.3
  • 23
    • 0035808385 scopus 로고    scopus 로고
    • The forkhead-associated domain of NBS1 is essential for nuclear foci formation after irradiation but not essential for hRAD50/hMRE11/NBS1 complex DNA repair activity
    • Tauchi, H., Kobayashi, J., Morishima, K., Matsuura, S., Nakamura, A., Shiraishi, T., Ito, E., Masnada, D., Delia, D., and Komatsu, K. (2001) The forkhead-associated domain of NBS1 is essential for nuclear foci formation after irradiation but not essential for hRAD50/hMRE11/NBS1 complex DNA repair activity. J. Biol. Chem. 276, 12-15.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12-15
    • Tauchi, H.1    Kobayashi, J.2    Morishima, K.3    Matsuura, S.4    Nakamura, A.5    Shiraishi, T.6    Ito, E.7    Masnada, D.8    Delia, D.9    Komatsu, K.10
  • 24
    • 0034721154 scopus 로고    scopus 로고
    • Chfr defines a mitotic stress checkpoint that delays entry into metaphase
    • Scolnick, D.M., and Halazonetis, T.D. (2000) Chfr defines a mitotic stress checkpoint that delays entry into metaphase. Nature 406, 430-435.
    • (2000) Nature , vol.406 , pp. 430-435
    • Scolnick, D.M.1    Halazonetis, T.D.2
  • 25
    • 0037148527 scopus 로고    scopus 로고
    • The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition
    • Kang, D., Chen, J., Wong, J., and Fang, G. (2002) The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition. J. Cell Biol. 156, 249-259.
    • (2002) J. Cell Biol. , vol.156 , pp. 249-259
    • Kang, D.1    Chen, J.2    Wong, J.3    Fang, G.4
  • 26
    • 0343442520 scopus 로고    scopus 로고
    • Forkhead transcription factors, Fkh1p and Fkh2p, collaborate with Mcm1p to control transcription required for M-phase
    • Kumar, R., Reynolds, D.M., Shevchenko, A., Goldstone, S.D., and Dalton, S. (2000) Forkhead transcription factors, Fkh1p and Fkh2p, collaborate with Mcm1p to control transcription required for M-phase. Curr. Biol. 10, 896-906.
    • (2000) Curr. Biol. , vol.10 , pp. 896-906
    • Kumar, R.1    Reynolds, D.M.2    Shevchenko, A.3    Goldstone, S.D.4    Dalton, S.5
  • 27
    • 0034650839 scopus 로고    scopus 로고
    • The winged-helix/forkhead protein myocyte nuclear factor beta, MNF-beta) forms a co-repressor complex with mammalian sin3B
    • Yang, Q., Kong, Y., Rothermel, B., Garry, D.J., Bassel-Duby, R., and Williams, R.S. (2000) The winged-helix/forkhead protein myocyte nuclear factor beta, MNF-beta) forms a co-repressor complex with mammalian sin3B. Biochem. J. 345, 335-343.
    • (2000) Biochem. J. , vol.345 , pp. 335-343
    • Yang, Q.1    Kong, Y.2    Rothermel, B.3    Garry, D.J.4    Bassel-Duby, R.5    Williams, R.S.6
  • 28
    • 0034672623 scopus 로고    scopus 로고
    • Kinesin subfamily UNC104 contains a FHA domain: Boundaries and physicochemical characterization
    • Westerholm-Parvinen, A., Vernos, I., and Serrano, L. (2000) Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization. FEBS Lett. 486, 285-290.
    • (2000) FEBS Lett. , vol.486 , pp. 285-290
    • Westerholm-Parvinen, A.1    Vernos, I.2    Serrano, L.3
  • 29
    • 0037081776 scopus 로고    scopus 로고
    • Signal- and importin-dependent nuclear targeting of the kidney anion exchanger 1-binding protein kanadaptin
    • Hubner, S., Jans, D.A., Xiao, C.Y., John, A.P., and Drenckhahn, D. (2002) Signal- and importin-dependent nuclear targeting of the kidney anion exchanger 1-binding protein kanadaptin. Biochem. J. 361, 287-296.
    • (2002) Biochem. J. , vol.361 , pp. 287-296
    • Hubner, S.1    Jans, D.A.2    Xiao, C.Y.3    John, A.P.4    Drenckhahn, D.5
  • 31
    • 0035816641 scopus 로고    scopus 로고
    • A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis
    • Takagi, M., Sueishi, M., Saiwaki, T., Kametaka, A., and Yoneda, Y. (2001) A novel nucleolar protein, NIFK, interacts with the forkhead associated domain of Ki-67 antigen in mitosis. J. Biol. Chem. 276, 25386-25391.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25386-25391
    • Takagi, M.1    Sueishi, M.2    Saiwaki, T.3    Kametaka, A.4    Yoneda, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.