The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study

被引：9
作者：
Schmidtmann, A [1 ]
Lohmann, K [1 ]
Jaquet, K [1 ]
机构：
[1] Ruhr Univ Bochum, Fak Med, Biochem Supramolek Syst Abt, D-44780 Bochum, Germany
来源：
FEBS LETTERS | 2002年 / 513卷 / 2-3期
关键词：
P-31-nuclear magnetic resonance; cardiac troponin; cardiac troponin I; cardiac troponin C; cardiac troponin T;
D O I：
10.1016/S0014-5793(02)02340-2
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cardiac troponin I, the inhibitory subunit of the heterotrimeric cardiac troponin (cTn) complex is phosphorylated by protein kinase A at two serine residues located in its heart-specific NI-terminal extension. This flexible arm interacts at different sites within cTn dependent on its phosphorylation degree. BisphosphoryIation is known to induce conformational changes within cTnI which finally lead to a reduction of the calcium affinity of cTnC. However, as we show here, the bisphosphorylated cTnI arm does not interact with cTnC, but with cTnT and/or cTnI. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码：289 / 293
页数：5
相关论文
共 30 条
  • [1] Modulation of cardiac troponin C-cardiac troponin I regulatory interactions by the amino-terminus of cardiac troponin I
    Abbott, MB
    Dong, WJ
    Dvoretsky, A
    DaGue, B
    Caprioli, RM
    Cheung, HC
    Rosevear, PR
    [J]. BIOCHEMISTRY, 2001, 40 (20) : 5992 - 6001
  • [2] Microanalysis and distribution of cardiac troponin I phospho species in heart areas
    Ardelt, P
    Dorka, P
    Jaquet, K
    Heilmeyer, LMG
    Körtke, H
    Körfer, R
    Notohamiprodjo, G
    [J]. BIOLOGICAL CHEMISTRY, 1998, 379 (03) : 341 - 347
  • [3] BABU A, 1992, J BIOL CHEM, V267, P15469
  • [4] ISOLATION AND CHARACTERIZATION OF A HIGHLY PHOSPHORYLATED TROPONIN FROM BOVINE HEART
    BEIER, N
    JAQUET, K
    SCHNACKERZ, K
    HEILMEYER, LMG
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 176 (02): : 327 - 334
  • [5] Effects of protein kinase A phosphorylation on signaling between cardiac troponin I and the N-terminal domain of cardiac troponin C
    Chandra, M
    Dong, WJ
    Pan, BS
    Cheung, HC
    Solaro, RJ
    [J]. BIOCHEMISTRY, 1997, 36 (43) : 13305 - 13311
  • [6] Effects of phosphorylation and mutation R145G on human cardiac troponin I function
    Deng, Y
    Schmidtmann, A
    Redlich, A
    Westerdorf, B
    Jaquet, K
    Thieleczek, R
    [J]. BIOCHEMISTRY, 2001, 40 (48) : 14593 - 14602
  • [7] Conformation of the N-terminal segment of a monocysteine mutant of troponin I from cardiac muscle
    Dong, WJ
    Chandra, M
    Xing, J
    Solaro, RJ
    Cheung, HC
    [J]. BIOCHEMISTRY, 1997, 36 (22) : 6745 - 6753
  • [8] CORRELATION BETWEEN CONTRACTION AND PHOSPHORYLATION OF INHIBITORY SUBUNIT OF TROPONIN IN PERFUSED RAT-HEART
    ENGLAND, PJ
    [J]. FEBS LETTERS, 1975, 50 (01): : 57 - 60
  • [9] Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C:: N- and C-terminal low affinity contributing regions
    Ferrières, G
    Pugnière, M
    Mani, JC
    Villard, S
    Laprade, M
    Doutre, P
    Pau, B
    Granier, C
    [J]. FEBS LETTERS, 2000, 479 (03) : 99 - 105
  • [10] DIFFERENTIAL EXPRESSION OF SLOW AND FAST SKELETAL-MUSCLE TROPONIN-C - SLOW SKELETAL-MUSCLE TROPONIN-C IS EXPRESSED IN HUMAN-FIBROBLASTS
    GAHLMANN, R
    WADE, R
    GUNNING, P
    KEDES, L
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1988, 201 (02) : 379 - 391
123