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连接区SR蛋白JP-45影响电压依赖性Ca2+通道Cav1.1的功能表达。

The junctional SR protein JP-45 affects the functional expression of the voltage-dependent Ca2+ channel Cav1.1.

作者信息

Anderson Ayuk A, Altafaj Xavier, Zheng Zhenlin, Wang Zhong-Min, Delbono Osvaldo, Ronjat Michel, Treves Susan, Zorzato Francesco

机构信息

Department of Anaesthesia, Basel University Hospital, Hebelstrasse 20, 4031 Basel, Switzerland.

出版信息

J Cell Sci. 2006 May 15;119(Pt 10):2145-55. doi: 10.1242/jcs.02935. Epub 2006 Apr 25.

DOI:10.1242/jcs.02935
PMID:16638807
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2802288/
Abstract

JP-45, an integral protein of the junctional face membrane of the skeletal muscle sarcoplasmic reticulum (SR), colocalizes with its Ca2+ -release channel (the ryanodine receptor), and interacts with calsequestrin and the skeletal-muscle dihydropyridine receptor Cav1. We have identified the domains of JP-45 and the Cav1.1 involved in this interaction, and investigated the functional effect of JP-45. The cytoplasmic domain of JP-45, comprising residues 1-80, interacts with Cav1.1. JP-45 interacts with two distinct and functionally relevant domains of Cav1.1, the I-II loop and the C-terminal region. Interaction between JP-45 and the I-II loop occurs through the alpha-interacting domain in the I-II loop. beta1a, a Cav1 subunit, also interacts with the cytosolic domain of JP-45, and its presence drastically reduces the interaction between JP-45 and the I-II loop. The functional effect of JP-45 on Cav1.1 activity was assessed by investigating charge movement in differentiated C2C12 myotubes after overexpression or depletion of JP-45. Overexpression of JP-45 decreased peak charge-movement and shifted VQ1/2 to a more negative potential (-10 mV). JP-45 depletion decreased both the content of Cav1.1 and peak charge-movements. Our data demonstrate that JP-45 is an important protein for functional expression of voltage-dependent Ca2+ channels.

摘要

JP - 45是骨骼肌肌浆网（SR）连接面膜的一种整合蛋白，与它的钙离子释放通道（兰尼碱受体）共定位，并与肌集钙蛋白和骨骼肌二氢吡啶受体Cav1相互作用。我们已经确定了参与这种相互作用的JP - 45和Cav1.1的结构域，并研究了JP - 45的功能作用。JP - 45的胞质结构域，由1 - 80位残基组成，与Cav1.1相互作用。JP - 45与Cav1.1的两个不同且功能相关的结构域相互作用，即I - II环和C末端区域。JP - 45与I - II环之间的相互作用通过I - II环中的α相互作用结构域发生。Cav1亚基β1a也与JP - 45的胞质结构域相互作用，并且它的存在极大地降低了JP - 45与I - II环之间的相互作用。通过研究过表达或缺失JP - 45后分化的C2C12肌管中的电荷移动，评估了JP - 45对Cav1.1活性的功能作用。JP - 45的过表达降低了峰值电荷移动，并使VQ1/2向更负的电位（-10 mV）移动。JP - 45的缺失降低了Cav1.1的含量和峰值电荷移动。我们的数据表明，JP - 45是电压依赖性钙离子通道功能表达的重要蛋白。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/c9042f3a8774/halms381691f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/6fd199ccedb1/halms381691f1.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/9e2a3a171f51/halms381691f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/617124dbaa4c/halms381691f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/f723a3c5087d/halms381691f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/8fc0ba6e8774/halms381691f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/b09bfe0d3876/halms381691f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/5e334415409c/halms381691f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/91394a22f593/halms381691f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/c9042f3a8774/halms381691f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/6fd199ccedb1/halms381691f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/c9efd647c406/halms381691f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/9e2a3a171f51/halms381691f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/617124dbaa4c/halms381691f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/f723a3c5087d/halms381691f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/8fc0ba6e8774/halms381691f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/b09bfe0d3876/halms381691f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/5e334415409c/halms381691f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/91394a22f593/halms381691f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7523/2802288/c9042f3a8774/halms381691f10.jpg

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