메뉴 건너뛰기




Volumn 50, Issue 12, 2011, Pages 2187-2193

Phosphorylation of annexin A1 by TRPM7 kinase: A switch regulating the induction of an α-helix

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC; ANNEXINS; BIFUNCTIONAL PROTEINS; HELICAL CONFORMATION; ION CHANNEL; KINASE DOMAINS; MEMBRANE BINDING; MEMBRANE TRAFFICKING; N-TERMINALS; PHOSPHOLIPID VESICLES;

EID: 79952927802     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101963h     Document Type: Article
Times cited : (42)

References (28)
  • 2
    • 0037065734 scopus 로고    scopus 로고
    • Effect of phosphorylation on α-helix stability as a function of position
    • DOI 10.1021/bi0113216
    • Andrew, C. D., Warwicker, J., Jones, G. R., and Doig, A. J. (2002) Effect of phosphorylation on α-helix stability as a function of position Biochemistry 41, 1897-1905 (Pubitemid 34132265)
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1897-1905
    • Andrew, C.D.1    Warwicker, J.2    Jones, G.R.3    Doig, A.J.4
  • 4
    • 0033611493 scopus 로고    scopus 로고
    • α-Kinases: A new class of protein kinases with a novel catalytic domain
    • Ryazanov, A. G., Pavur, K. S., and Dorovkov, M. V. (1999) α-Kinases: A new class of protein kinases with a novel catalytic domain Curr. Biol. 9, R43-R45
    • (1999) Curr. Biol. , vol.9
    • Ryazanov, A.G.1    Pavur, K.S.2    Dorovkov, M.V.3
  • 5
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • Pinna, L. A. and Ruzzene, M. (1996) How do protein kinases recognize their substrates? Biochim. Biophys. Acta 1314, 191-225
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 6
    • 1842536165 scopus 로고    scopus 로고
    • Alpha-kinases: Analysis of the family and comparison with conventional protein kinases
    • DOI 10.1016/S0079-6107(03)00060-9, PII S0079610703000609
    • Drennan, D. and Ryazanov, A. G. (2004) α-Kinases: Analysis of the family and comparison with conventional protein kinases Prog. Biophys. Mol. Biol. 85, 1-32 (Pubitemid 38431208)
    • (2004) Progress in Biophysics and Molecular Biology , vol.85 , Issue.1 , pp. 1-32
    • Drennan, D.1    Ryazanov, A.G.2
  • 8
    • 10944269137 scopus 로고    scopus 로고
    • Phosphorylation of annexin I by TRPM7 channel-kinase
    • DOI 10.1074/jbc.C400441200
    • Dorovkov, M. V. and Ryazanov, A. G. (2004) Phosphorylation of annexin I by TRPM7 channel-kinase J. Biol. Chem. 279, 50643-50646 (Pubitemid 40017798)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50643-50646
    • Dorovkov, M.V.1    Ryazanov, A.G.2
  • 9
    • 41449095709 scopus 로고    scopus 로고
    • Membrane-induced folding and structure of membrane-bound annexin A1 N-terminal peptides: Implications for annexin-induced membrane aggregation
    • Hu, N. J., Bradshaw, J., Lauter, H., Buckingham, J., Solito, E., and Hofmann, A. (2008) Membrane-induced folding and structure of membrane-bound annexin A1 N-terminal peptides: Implications for annexin-induced membrane aggregation Biophys. J. 94, 1773-1781
    • (2008) Biophys. J. , vol.94 , pp. 1773-1781
    • Hu, N.J.1    Bradshaw, J.2    Lauter, H.3    Buckingham, J.4    Solito, E.5    Hofmann, A.6
  • 11
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V. and Moss, S. E. (2002) Annexins: From structure to function Physiol. Rev. 82, 331-371 (Pubitemid 34654456)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 13
    • 0035936691 scopus 로고    scopus 로고
    • X-ray structure of full-length annexin 1 and implications for membrane aggregation
    • DOI 10.1006/jmbi.2000.4423
    • Rosengarth, A., Gerke, V., and Luecke, H. (2001) X-ray structure of full-length annexin 1 and implications for membrane aggregation J. Mol. Biol. 306, 489-498 (Pubitemid 33027717)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.3 , pp. 489-498
    • Rosengarth, A.1    Gerke, V.2    Luecke, H.3
  • 14
    • 0037424618 scopus 로고    scopus 로고
    • A calcium-driven conformational switch of the N-terminal and core domains of annexin A1
    • DOI 10.1016/S0022-2836(03)00027-5
    • Rosengarth, A. and Luecke, H. (2003) A calcium-driven conformational switch of the N-terminal and core domains of annexin A1 J. Mol. Biol. 326, 1317-1325 (Pubitemid 36269076)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.5 , pp. 1317-1325
    • Rosengarth, A.1    Luecke, H.2
  • 15
    • 0029811498 scopus 로고    scopus 로고
    • Structural requirements for annexin I-S100C complex-formation
    • Seemann, J., Weber, K., and Gerke, V. (1996) Structural requirements for annexin I-S100C complex-formation Biochem. J. 319, 123-129 (Pubitemid 26394748)
    • (1996) Biochemical Journal , vol.319 , Issue.1 , pp. 123-129
    • Seemann, J.1    Weber, K.2    Gerke, V.3
  • 16
    • 0038342516 scopus 로고    scopus 로고
    • Unmasking the annexin I interaction from the structure of apo-S100A11
    • DOI 10.1016/S0969-2126(03)00126-6
    • Dempsey, A. C., Walsh, M. P., and Shaw, G. S. (2003) Unmasking the annexin I interaction from the structure of Apo-S100A11 Structure 11, 887-897 (Pubitemid 36830848)
    • (2003) Structure , vol.11 , Issue.7 , pp. 887-897
    • Dempsey, A.C.1    Walsh, M.P.2    Shaw, G.S.3
  • 17
    • 0034634564 scopus 로고    scopus 로고
    • Solution structure and membrane-binding property of the N-terminal tail domain of human annexin i
    • Yoon, M. K., Park, S. H., Won, H. S., Na, D. S., and Lee, B. J. (2000) Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I FEBS Lett. 484, 241-245
    • (2000) FEBS Lett. , vol.484 , pp. 241-245
    • Yoon, M.K.1    Park, S.H.2    Won, H.S.3    Na, D.S.4    Lee, B.J.5
  • 18
    • 0028672795 scopus 로고
    • Methods to study membrane protein structure in solution
    • Henry, G. D. and Sykes, B. D. (1994) Methods to study membrane protein structure in solution Methods Enzymol. 239, 515-535
    • (1994) Methods Enzymol. , vol.239 , pp. 515-535
    • Henry, G.D.1    Sykes, B.D.2
  • 21
    • 0029143230 scopus 로고
    • Vesicle aggregation by annexin I: Role of a secondary membrane binding site
    • de la Fuente, M. and Parra, A. V. (1995) Vesicle aggregation by annexin I: Role of a secondary membrane binding site Biochemistry 34, 10393-10399
    • (1995) Biochemistry , vol.34 , pp. 10393-10399
    • De La Fuente, M.1    Parra, A.V.2
  • 22
    • 0034619577 scopus 로고    scopus 로고
    • Mechanism of annexin I-mediated membrane aggregation
    • Bitto, E., Li, M., Tikhonov, A. M., Schlossman, M. L., and Cho, W. (2000) Mechanism of annexin I-mediated membrane aggregation Biochemistry 39, 13469-13477
    • (2000) Biochemistry , vol.39 , pp. 13469-13477
    • Bitto, E.1    Li, M.2    Tikhonov, A.M.3    Schlossman, M.L.4    Cho, W.5
  • 23
    • 65249168645 scopus 로고    scopus 로고
    • Annexin i and annexin II N-terminal peptides binding to S100 protein family members: Specificity and thermodynamic characterization
    • Streicher, W. W., Lopez, M. M., and Makhatadze, G. I. (2009) Annexin I and annexin II N-terminal peptides binding to S100 protein family members: Specificity and thermodynamic characterization Biochemistry 48, 2788-2798
    • (2009) Biochemistry , vol.48 , pp. 2788-2798
    • Streicher, W.W.1    Lopez, M.M.2    Makhatadze, G.I.3
  • 24
    • 4344568113 scopus 로고    scopus 로고
    • Scrutiny of annexin A1 mediated membrane-membrane interaction by means of a thickness shear mode resonator and computer simulations
    • Kastl, K., Herrig, A., Luthgens, E., Janshoff, A., and Steinem, C. (2004) Scrutiny of annexin A1 mediated membrane-membrane interaction by means of a thickness shear mode resonator and computer simulations Langmuir 20, 7246-7253
    • (2004) Langmuir , vol.20 , pp. 7246-7253
    • Kastl, K.1    Herrig, A.2    Luthgens, E.3    Janshoff, A.4    Steinem, C.5
  • 25
    • 0033521226 scopus 로고    scopus 로고
    • Thermodynamics of the α-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium
    • Wieprecht, T., Apostolov, O., Beyermann, M., and Seelig, J. (1999) Thermodynamics of the α-helix-coil transition of amphipathic peptides in a membrane environment: Implications for the peptide-membrane binding equilibrium J. Mol. Biol. 294, 785-794
    • (1999) J. Mol. Biol. , vol.294 , pp. 785-794
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 27
    • 4644281168 scopus 로고    scopus 로고
    • An N-terminal amphipathic helix in Hepatitis C Virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication
    • DOI 10.1128/JVI.78.20.11393-11400.2004
    • Elazar, M., Liu, P., Rice, C. M., and Glenn, J. S. (2004) An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication J. Virol. 78, 11393-11400 (Pubitemid 39299681)
    • (2004) Journal of Virology , vol.78 , Issue.20 , pp. 11393-11400
    • Elazar, M.1    Liu, P.2    Rice, C.M.3    Glenn, J.S.4
  • 28
    • 78049319504 scopus 로고    scopus 로고
    • A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
    • Karanasios, E., Han, G. S., Xu, Z., Carman, G. M., and Siniossoglou, S. (2010) A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase Proc. Natl. Acad. Sci. U.S.A. 107, 17539-17544
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17539-17544
    • Karanasios, E.1    Han, G.S.2    Xu, Z.3    Carman, G.M.4    Siniossoglou, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.