Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum-Reference-Cited by-同舟云学术

Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

Published:2009-08-01 Issue:15 Volume:122 Page:2640-2650
ISSN:1477-9137
Container-title:Journal of Cell Science
language:en
Short-container-title:

Author:

Lange Stephan¹,Ouyang Kunfu¹,Meyer Gretchen²³,Cui Li¹,Cheng Hongqiang¹,Lieber Richard L.²³,Chen Ju¹

Affiliation:

1. Department of Medicine, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA

2. Departments of Orthopedic Surgery and Bioengineering, University of California, La Jolla, CA 92093, USA

3. VA Medical Center, San Diego, CA 92161, USA

Abstract

The giant protein obscurin is thought to link the sarcomere with the sarcoplasmic reticulum (SR). The N-terminus of obscurin interacts with the M-band proteins titin and myomesin, whereas the C-terminus mediates interactions with ankyrin proteins. Here, we investigate the importance of obscurin for SR architecture and organization. Lack of obscurin in cross-striated muscles leads to changes in longitudinal SR architecture and disruption of small ankyrin-1.5 (sAnk1.5) expression and localization. Changes in SR architecture in obscurin knockout mice are also associated with alterations in several SR or SR-associated proteins, such as ankyrin-2 and β-spectrin. Finally, obscurin knockout mice display centralized nuclei in skeletal muscles as a sign of mild myopathy, but have normal sarcomeric structure and preserved muscle function.

Publisher

The Company of Biologists

Subject

Cell Biology

Link

http://journals.biologists.com/jcs/article-pdf/122/15/2640/1561959/2640.pdf

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