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Author Notes:
*Corresponding author, barsteadr@omrf.ouhsc.edu.
The mass spectrometric analyses were performed by the Emory University Proteomics Core Service Center.
We appreciate the help of the Core’s director, Dr. Junmin Peng.
HL is a Sloan Foundation fellow in neuroscience.
Subjects:
Research Funding:
This work was supported by a grant from the Muscular Dystrophy Association of America to RJB, and grant AR052133 from the National Institutes of Health to GMB.
Keywords:
- Science & Technology
- Life Sciences & Biomedicine
- Biochemistry & Molecular Biology
- alpha-actinin
- focal adhesion
- muscle
- Caenorhabditis elegans
- FOCAL SEGMENTAL GLOMERULOSCLEROSIS
- VINCULIN-BINDING-SITE
- C-ELEGANS
- INTRAMOLECULAR ASSOCIATION
- MUSCULAR-DYSTROPHY
- SPECTRIN REPEAT
- TALIN CONTAINS
- TAIL DOMAINS
- DENSE-BODY
- MUSCLE
alpha-Actinin Is Required for the Proper Assembly of Z-Disk/Focal-Adhesion-Like Structures and for Efficient Locomotion in Caenorhabditis elegans
Abstract:
The actin binding protein α-actinin is a major component of focal adhesions found in vertebrate cells and of focal-adhesion-like structures found in the body wall muscle of the nematode Caenorhabditis elegans. To study its in vivo function in this genetic model system, we isolated a strain carrying a deletion of the single C. elegans α-actinin gene. We assessed the cytological organization of other C. elegans focal adhesion proteins and the ultrastructure of the mutant. The mutant does not have normal dense bodies, as observed by electron microscopy; however, these dense-body-like structures still contain the focal adhesion proteins integrin, talin, and vinculin, as observed by immunofluorescence microscopy. Actin is found in normal-appearing I-bands, but with abnormal accumulations near muscle cell membranes. Although swimming in water appeared grossly normal, use of automated methods for tracking the locomotion of individual worms revealed a defect in bending. We propose that the reduced motility of α-actinin null is due to abnormal dense bodies that are less able to transmit the forces generated by actin/myosin interactions.
Copyright information:
© 2010 Elsevier Ltd.
This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (http://creativecommons.org/licenses/by-nc-nd/4.0/).
