Ca2+ sensors of L‐type Ca2+ channel

FEBS Letters

Schaufler, Daniela²  Abernethy, Darrell R.¹  Kahr, Heike²  Romanin, Christoph²  Soldatov, Nikolai M.¹  Carlson, Olga¹  Gamsjaeger, Roland² 

[1] National Institute on Aging, NIH, 5600 Nathan Shock Drive, Baltimore, MD 21224-6825, USA;Institute for Biophysics, University of Linz, Altenbergerstrasse 69, A-4040 Linz, Austria

关键词: Heart;    Calcium channel;    Calmodulin;    Ca2+ sensor;    Inactivation;    CaM;    calmodulin;    GST;    glutathione S-transferase;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(00)02361-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Ca²⁺-induced inactivation of L-type Ca²⁺ is differentially mediated by two C-terminal motifs of the α_1C subunit, L (1572–1587) and K (1599–1651) implicated for calmodulin binding. We found that motif L is composed of a highly selective Ca²⁺ sensor and an adjacent Ca²⁺-independent tethering site for calmodulin. The Ca²⁺ sensor contributes to higher Ca²⁺ sensitivity of the motif L complex with calmodulin. Since only combined mutation of both sites removes Ca²⁺-dependent current decay, the two-site modulation by Ca²⁺ and calmodulin may underlie Ca²⁺-induced inactivation of the channel.

【 授权许可】

Unknown