메뉴 건너뛰기




Volumn 424, Issue 1-2, 2012, Pages 88-103

Directed evolution of the forkhead-associated domain to generate anti-phosphospecific reagents by phage display

Author keywords

affinity selection; alanine scanning; FHA1 libraries; isothermal calorimetry; phosphothreonine peptides

Indexed keywords

CHECKPOINT KINASE 2; FORKHEAD TRANSCRIPTION FACTOR; PHOSPHOTHREONINE; REAGENT; TRANSCRIPTION FACTOR FHA1; UNCLASSIFIED DRUG;

EID: 84868207373     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.09.006     Document Type: Article
Times cited : (11)

References (45)
  • 2
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture
    • P. Cohen The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture Eur. J. Biochem. 268 2001 5001 5010
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 4
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • M.B. Yaffe, and A.E. Elia Phosphoserine/threonine-binding domains Curr. Opin. Cell Biol. 13 2001 131 138
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.2
  • 5
    • 0042203565 scopus 로고    scopus 로고
    • SH2 and PTB domains in tyrosine kinase signaling
    • J. Schlessinger, and M.A. Lemmon SH2 and PTB domains in tyrosine kinase signaling Sci. STKE 2003 RE12
    • (2003) Sci. STKE , pp. 12
    • Schlessinger, J.1    Lemmon, M.A.2
  • 6
    • 0036518996 scopus 로고    scopus 로고
    • Phosphotyrosine-binding domains in signal transduction
    • M.B. Yaffe Phosphotyrosine-binding domains in signal transduction Nat. Rev. Mol. Cell Biol. 3 2002 177 186
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 177-186
    • Yaffe, M.B.1
  • 7
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • A.J. Muslin, J.W. Tanner, P.M. Allen, and A.S. Shaw Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine Cell 84 1996 889 897
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 8
    • 19344376145 scopus 로고    scopus 로고
    • 14-3-3 proteins: A number of functions for a numbered protein
    • D. Bridges, and G.B. Moorhead 14-3-3 proteins: a number of functions for a numbered protein Sci. STKE 2005 re10
    • (2005) Sci. STKE , pp. 10
    • Bridges, D.1    Moorhead, G.B.2
  • 9
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • P.J. Lu, X.Z. Zhou, M. Shen, and K.P. Lu Function of WW domains as phosphoserine- or phosphothreonine-binding modules Science 283 1999 1325 1328
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 10
    • 0034531364 scopus 로고    scopus 로고
    • The FHA domain mediates phosphoprotein interactions
    • J. Li, G.I. Lee, S.R. Van Doren, and J.C. Walker The FHA domain mediates phosphoprotein interactions J. Cell Sci. 113 2000 4143 4149
    • (2000) J. Cell Sci. , vol.113 , pp. 4143-4149
    • Li, J.1    Lee, G.I.2    Van Doren, S.R.3    Walker, J.C.4
  • 11
    • 0036070545 scopus 로고    scopus 로고
    • FHA: A signal transduction domain with diverse specificity and function
    • M.D. Tsai FHA: a signal transduction domain with diverse specificity and function Structure 10 2002 887 888
    • (2002) Structure , vol.10 , pp. 887-888
    • Tsai, M.D.1
  • 13
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • D. Skowyra, K.L. Craig, M. Tyers, S.J. Elledge, and J.W. Harper F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex Cell 91 1997 209 219
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 14
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • T. Pawson, and P. Nash Assembly of cell regulatory systems through protein interaction domains Science 300 2003 445 452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 15
    • 68249125947 scopus 로고    scopus 로고
    • 14-3-3 proteins, FHA domains and BRCT domains in the DNA damage response
    • D.H. Mohammad, and M.B. Yaffe 14-3-3 proteins, FHA domains and BRCT domains in the DNA damage response DNA Repair (Amst) 8 2009 1009 1017
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1009-1017
    • Mohammad, D.H.1    Yaffe, M.B.2
  • 16
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • D. Durocher, J. Henckel, A.R. Fersht, and S.P. Jackson The FHA domain is a modular phosphopeptide recognition motif Mol. Cell 4 1999 387 394
    • (1999) Mol. Cell , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Fersht, A.R.3    Jackson, S.P.4
  • 17
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • D. Durocher, I.A. Taylor, D. Sarbassova, L.F. Haire, S.L. Westcott, and S.P. Jackson The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms Mol. Cell 6 2000 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
  • 18
    • 0034671365 scopus 로고    scopus 로고
    • Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9
    • H. Liao, C. Yuan, M.I. Su, S. Yongkiettrakul, D. Qin, and H. Li Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9 J. Mol. Biol. 304 2000 941 951
    • (2000) J. Mol. Biol. , vol.304 , pp. 941-951
    • Liao, H.1    Yuan, C.2    Su, M.I.3    Yongkiettrakul, S.4    Qin, D.5    Li, H.6
  • 19
    • 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
    • I.J. Byeon, S. Yongkiettrakul, and M.D. Tsai 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 2001 577 588
    • (2001) J. Mol. Biol. , vol.314 , pp. 577-588
    • Byeon, I.J.1    Yongkiettrakul, S.2    Tsai, M.D.3
  • 20
    • 0034730367 scopus 로고    scopus 로고
    • II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides
    • P. Wang, I.J. Byeon, H. Liao, K.D. Beebe, S. Yongkiettrakul, D. Pei, and M.D. Tsai II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides J. Mol. Biol. 302 2000 927 940
    • (2000) J. Mol. Biol. , vol.302 , pp. 927-940
    • Wang, P.1    Byeon, I.J.2    Liao, H.3    Beebe, K.D.4    Yongkiettrakul, S.5    Pei, D.6    Tsai, M.D.7
  • 21
    • 0036285705 scopus 로고    scopus 로고
    • Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2
    • J. Li, B.L. Williams, L.F. Haire, M. Goldberg, E. Wilker, and D. Durocher Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2 Mol. Cell 9 2002 1045 1054
    • (2002) Mol. Cell , vol.9 , pp. 1045-1054
    • Li, J.1    Williams, B.L.2    Haire, L.F.3    Goldberg, M.4    Wilker, E.5    Durocher, D.6
  • 22
    • 44949170836 scopus 로고    scopus 로고
    • Diphosphothreonine-specific interaction between an SQ/TQ cluster and an FHA domain in the Rad53-Dun1 kinase cascade
    • H. Lee, C. Yuan, A. Hammet, A. Mahajan, E.S. Chen, and M.R. Wu Diphosphothreonine-specific interaction between an SQ/TQ cluster and an FHA domain in the Rad53-Dun1 kinase cascade Mol. Cell 30 2008 767 778
    • (2008) Mol. Cell , vol.30 , pp. 767-778
    • Lee, H.1    Yuan, C.2    Hammet, A.3    Mahajan, A.4    Chen, E.S.5    Wu, M.R.6
  • 23
    • 0344255640 scopus 로고    scopus 로고
    • Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions
    • H. Li, I.J. Byeon, Y. Ju, and M.D. Tsai Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions J. Mol. Biol. 335 2004 371 381
    • (2004) J. Mol. Biol. , vol.335 , pp. 371-381
    • Li, H.1    Byeon, I.J.2    Ju, Y.3    Tsai, M.D.4
  • 24
    • 1842435001 scopus 로고    scopus 로고
    • The ligand specificity of yeast Rad53 FHA domains at the + 3 position is determined by nonconserved residues
    • S. Yongkiettrakul, I.J. Byeon, and M.D. Tsai The ligand specificity of yeast Rad53 FHA domains at the + 3 position is determined by nonconserved residues Biochemistry 43 2004 3862 3869
    • (2004) Biochemistry , vol.43 , pp. 3862-3869
    • Yongkiettrakul, S.1    Byeon, I.J.2    Tsai, M.D.3
  • 25
    • 78649766290 scopus 로고    scopus 로고
    • Structural and functional analysis of phosphothreonine-dependent FHA domain interactions
    • S. Pennell, S. Westcott, M. Ortiz-Lombardia, D. Patel, J. Li, and T.J. Nott Structural and functional analysis of phosphothreonine-dependent FHA domain interactions Structure 18 2010 1587 1595
    • (2010) Structure , vol.18 , pp. 1587-1595
    • Pennell, S.1    Westcott, S.2    Ortiz-Lombardia, M.3    Patel, D.4    Li, J.5    Nott, T.J.6
  • 26
    • 0034963561 scopus 로고    scopus 로고
    • Preparation and application of antibodies to phosphoamino acid sequences
    • T. Sun, M. Campbell, W. Gordon, and R.B. Arlinghaus Preparation and application of antibodies to phosphoamino acid sequences Biopolymers 60 2001 61 75
    • (2001) Biopolymers , vol.60 , pp. 61-75
    • Sun, T.1    Campbell, M.2    Gordon, W.3    Arlinghaus, R.B.4
  • 27
    • 0026470802 scopus 로고
    • Antiserum raised against a synthetic phosphotyrosine-containing peptide selectively recognizes p185neu/erbB-2 and the epidermal growth factor receptor
    • L. Bangalore, A.J. Tanner, A.P. Laudano, and D.F. Stern Antiserum raised against a synthetic phosphotyrosine-containing peptide selectively recognizes p185neu/erbB-2 and the epidermal growth factor receptor Proc. Natl Acad. Sci. USA 89 1992 11637 11641
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11637-11641
    • Bangalore, L.1    Tanner, A.J.2    Laudano, A.P.3    Stern, D.F.4
  • 28
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • M. Gebauer, and A. Skerra Engineered protein scaffolds as next-generation antibody therapeutics Curr. Opin. Chem. Biol. 13 2009 245 255
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 30
    • 84855616485 scopus 로고    scopus 로고
    • Improving expression of scFv fragments by co-expression of periplasmic chaperones
    • R. Kontermann, S. Dubel, Springer-Verlag Berlin, Heidelberg
    • J.V. Schaefer, and A. Pluckthun Improving expression of scFv fragments by co-expression of periplasmic chaperones R. Kontermann, S. Dubel, Antibody Engineering Vol. 2 2010 Springer-Verlag Berlin, Heidelberg 345 361
    • (2010) Antibody Engineering , vol.2 , pp. 345-361
    • Schaefer, J.V.1    Pluckthun, A.2
  • 31
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • C.F. Schierle, M. Berkmen, D. Huber, C. Kumamoto, D. Boyd, and J. Beckwith The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway J. Bacteriol. 185 2003 5706 5713
    • (2003) J. Bacteriol. , vol.185 , pp. 5706-5713
    • Schierle, C.F.1    Berkmen, M.2    Huber, D.3    Kumamoto, C.4    Boyd, D.5    Beckwith, J.6
  • 32
    • 17044426359 scopus 로고    scopus 로고
    • A twin-arginine translocation (Tat)-mediated phage display system
    • M. Paschke, and W. Hohne A twin-arginine translocation (Tat)-mediated phage display system Gene 350 2005 79 88
    • (2005) Gene , vol.350 , pp. 79-88
    • Paschke, M.1    Hohne, W.2
  • 33
    • 0033996321 scopus 로고    scopus 로고
    • Bacterial twin-arginine signal peptide-dependent protein translocation pathway: Evolution and mechanism
    • L.F. Wu, B. Ize, A. Chanal, Y. Quentin, and G. Fichant Bacterial twin-arginine signal peptide-dependent protein translocation pathway: evolution and mechanism J. Mol. Microbiol. Biotechnol. 2 2000 179 189
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 179-189
    • Wu, L.F.1    Ize, B.2    Chanal, A.3    Quentin, Y.4    Fichant, G.5
  • 34
    • 79956126348 scopus 로고    scopus 로고
    • Efficient phage display of intracellularly folded proteins mediated by the TAT pathway
    • J. Speck, K.M. Arndt, and K.M. Muller Efficient phage display of intracellularly folded proteins mediated by the TAT pathway Protein Eng. Des. Sel. 24 2011 473 484
    • (2011) Protein Eng. Des. Sel. , vol.24 , pp. 473-484
    • Speck, J.1    Arndt, K.M.2    Muller, K.M.3
  • 36
    • 58849105958 scopus 로고    scopus 로고
    • Functional assignment of solute-binding proteins of ABC transporters using a fluorescence-based thermal shift assay
    • S.E. Giuliani, A.M. Frank, and F.R. Collart Functional assignment of solute-binding proteins of ABC transporters using a fluorescence-based thermal shift assay Biochemistry 47 2008 13974 13984
    • (2008) Biochemistry , vol.47 , pp. 13974-13984
    • Giuliani, S.E.1    Frank, A.M.2    Collart, F.R.3
  • 37
    • 84872674041 scopus 로고    scopus 로고
    • Generating thermally stable variants of protein domains through phage-display
    • (Accepted for publication)
    • Pershad, K. & Kay, B. (Accepted for publication). Generating thermally stable variants of protein domains through phage-display. Methods J.
    • Methods J.
    • Pershad, K.1    Kay, B.2
  • 38
    • 0033584889 scopus 로고    scopus 로고
    • Selection for improved protein stability by phage display
    • S. Jung, A. Honegger, and A. Pluckthun Selection for improved protein stability by phage display J. Mol. Biol. 294 1999 163 180
    • (1999) J. Mol. Biol. , vol.294 , pp. 163-180
    • Jung, S.1    Honegger, A.2    Pluckthun, A.3
  • 39
  • 40
    • 27144492267 scopus 로고    scopus 로고
    • FHA domain-ligand interactions: Importance of integrating chemical and biological approaches
    • A. Mahajan, C. Yuan, B.L. Pike, J. Heierhorst, C.F. Chang, and M.D. Tsai FHA domain-ligand interactions: importance of integrating chemical and biological approaches J. Am. Chem. Soc. 127 2005 14572 14573
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14572-14573
    • Mahajan, A.1    Yuan, C.2    Pike, B.L.3    Heierhorst, J.4    Chang, C.F.5    Tsai, M.D.6
  • 42
    • 79953219400 scopus 로고    scopus 로고
    • Drop-out phagemid vector for switching from phage displayed affinity reagents to expression formats
    • K. Pershad, M.A. Sullivan, and B.K. Kay Drop-out phagemid vector for switching from phage displayed affinity reagents to expression formats Anal. Biochem. 412 2011 210 216
    • (2011) Anal. Biochem. , vol.412 , pp. 210-216
    • Pershad, K.1    Sullivan, M.A.2    Kay, B.K.3
  • 43
    • 10744221449 scopus 로고    scopus 로고
    • The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain
    • A.E. Elia, P. Rellos, L.F. Haire, J.W. Chao, F.J. Ivins, and K. Hoepker The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain Cell 115 2003 83 95
    • (2003) Cell , vol.115 , pp. 83-95
    • Elia, A.E.1    Rellos, P.2    Haire, L.F.3    Chao, J.W.4    Ivins, F.J.5    Hoepker, K.6
  • 44
    • 2542490186 scopus 로고    scopus 로고
    • Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1
    • R.S. Williams, M.S. Lee, D.D. Hau, and J.N. Glover Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1 Nat. Struct. Mol. Biol. 11 2004 519 525
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 519-525
    • Williams, R.S.1    Lee, M.S.2    Hau, D.D.3    Glover, J.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.