The Ca2+-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel-Reference-Cited by-同舟云学术

The Ca2+-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel

Published:2014-01-23 Issue:5 Volume:588 Page:665-671
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Sun Wei,Feng Rui,Hu Huiyuan,Guo Feng,Gao Qinghua,Shao Dongxue,Yin Dandan,Wang Hongmei,Sun Xuefei,Zhao Meimi,Minobe Etsuko,Sun Yingxian,Jiao Guangyu,Kameyama Masaki,Hao Liying

Funder

Natural Science Foundation of China

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2014.01.019/fullpdf

Reference19 articles.

1. Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues;Takano;J. Biochem.,2000

2. The calpain system;Goll;Physiol. Rev.,2003

3. A cytoplasmic factor, calpastatin and ATP together reverse run-down of Ca2+ channel activity in guinea-pig heart;Hao;J. Physiol.,1999

4. Molecular determinant for run-down of L-type Ca2+ channels localized in the carboxyl terminus of the 1C subunit;Kepplinger;J. Physiol.,2000

5. Calpastatin domain L is involved in the regulation of L-type Ca2+ channels in guinea pig cardiac myocytes;Hao;Biochem. Biophys. Res. Commun.,2000

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