Direct interaction of Ca2+/calmodulin inhibits histone deacetylase 5 repressor core binding to myocyte enhancer factor 2

被引：33

作者：

Berger, I ^{[1
]}

Bieniossek, C ^{[1
]}

Schaffitzel, C ^{[1
]}

Hassler, M ^{[1
]}

Santelli, E ^{[1
]}

Richmond, TJ ^{[1
]}

机构：

[1] ETH Honggerberg, Inst Mol Biol & Biophys, ETH Zurich, CH-8093 Zurich, Switzerland

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2003年 / 278卷 / 20期

关键词：

D O I：

10.1074/jbc.M301646200

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：

Myocyte enhancer factor 2 (MEF2) proteins play a pivotal role in the differentiation of cardiac and skeletal muscle cells. MEF2 factors are regulated by histone deacetylase enzymes such as histone deacetylase 5 (HDAC5). HDAC5 in turn is responsive to Ca2+ signaling mediated by the intracellular calcium sensor calmodulin. Here a combination of proteolytic fragmentation, matrix-assisted laser desorption ionization mass spectrometry, Edman degradation, circular dichroism, gel filtration, and surface plasmon resonance studies is utilized to define and characterize a stable core domain of HDAC5 and to examine its interactions with MEF2a and calmodulin. Results from real time binding experiments provide evidence for direct interaction of Ca2+/calmodulin with HDAC5 inhibiting MEF2a association with this enzyme.

引用

页码：17625 / 17635

页数：11

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