help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Felder, E.
Right arrow Articles by Allen, P. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Felder, E.
Right arrow Articles by Allen, P. D.

Biophys J, June 2002, p. 3144-3149, Vol. 82, No. 6

Morphology and Molecular Composition of Sarcoplasmic Reticulum Surface Junctions in the Absence of DHPR and RyR in Mouse Skeletal Muscle

Edward Felder,* Feliciano Protasi,dagger Ronit Hirsch,dagger Clara Franzini-Armstrong,* and Paul D. Allendagger

 *Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6058; and  dagger Department of Anesthesiology, Brigham and Woman's Hospital, Boston, Massachusetts 02115 USA

Calcium release during excitation-contraction coupling of skeletal muscle cells is initiated by the functional interaction of the exterior membrane and the sarcoplasmic reticulum (SR), mediated by the "mechanical" coupling of ryanodine receptors (RyR) and dihydropyridine receptors (DHPR). RyR is the sarcoplasmic reticulum Ca2+ release channel and DHPR is an L-type calcium channel of exterior membranes (surface membrane and T tubules), which acts as the voltage sensor of excitation-contraction coupling. The two proteins communicate with each other at junctions between SR and exterior membranes called calcium release units and are associated with several proteins of which triadin and calsequestrin are the best characterized. Calcium release units are present in diaphragm muscles and hind limb derived primary cultures of double knock out mice lacking both DHPR and RyR. The junctions show coupling between exterior membranes and SR, and an apparently normal content and disposition of triadin and calsequestrin. Therefore SR-surface docking, targeting of triadin and calsequestrin to the junctional SR domains and the structural organization of the two latter proteins are not affected by lack of DHPR and RyR. Interestingly, simultaneous lack of the two major excitation-contraction coupling proteins results in decrease of calcium release units frequency in the diaphragm, compared with either single knockout mutation.

Biophys J, June 2002, p. 3144-3149, Vol. 82, No. 6
© 2002 by the Biophysical Society   0006-3495/02/06/3144/06  $2.00



This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
E. H. Lee, G. Cherednichenko, I. N. Pessah, and P. D. Allen
Functional Coupling between TRPC3 and RyR1 Regulates the Expressions of Key Triadic Proteins
J. Biol. Chem., April 14, 2006; 281(15): 10042 - 10048.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
R. G. Weiss, K. M. S. O'Connell, B. E. Flucher, P. D. Allen, M. Grabner, and R. T. Dirksen
Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling
Am J Physiol Cell Physiol, October 1, 2004; 287(4): C1094 - C1102.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
E. H. Lee, J. R. Lopez, J. Li, F. Protasi, I. N. Pessah, D. H. Kim, and P. D. Allen
Conformational coupling of DHPR and RyR1 in skeletal myotubes is influenced by long-range allosterism: evidence for a negative regulatory module
Am J Physiol Cell Physiol, January 1, 2004; 286(1): C179 - C189.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
B. S. Launikonis, M. Barnes, and D. G. Stephenson
Identification of the coupling between skeletal muscle store-operated Ca2+ entry and the inositol trisphosphate receptor
PNAS, March 4, 2003; 100(5): 2941 - 2944.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
P. Tijskens, G. Meissner, and C. Franzini-Armstrong
Location of Ryanodine and Dihydropyridine Receptors in Frog Myocardium
Biophys. J., February 1, 2003; 84(2): 1079 - 1092.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
R. Araya, J. L. Liberona, J. C. Cardenas, N. Riveros, M. Estrada, J. A. Powell, M. A. Carrasco, and E. Jaimovich
Dihydropyridine Receptors as Voltage Sensors for a Depolarization-evoked, IP3R-mediated, Slow Calcium Signal in Skeletal Muscle Cells
J. Gen. Physiol., December 30, 2002; 121(1): 3 - 16.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Biophysical Society.