Journal article
Cbl-associated protein regulates assembly and function of two tension-sensing structures in Drosophila
Development (Cambridge), Vol.140(3), pp.627-638
02/01/2013
DOI: 10.1242/dev.085100
PMCID: PMC3561792
PMID: 23293294
Abstract
Cbl-associated protein (CAP) localizes to focal adhesions and associates with numerous cytoskeletal proteins; however, its physiological roles remain unknown. Here, we demonstrate that Drosophila CAP regulates the organization of two actin-rich structures in Drosophila: muscle attachment sites (MASs), which connect somatic muscles to the body wall; and scolopale cells, which form an integral component of the fly chordotonal organs and mediate mechanosensation. Drosophila CAP mutants exhibit aberrant junctional invaginations and perturbation of the cytoskeletal organization at the MAS. CAP depletion also results in collapse of scolopale cells within chordotonal organs, leading to deficits in larval vibration sensation and adult hearing. We investigate the roles of different CAP protein domains in its recruitment to, and function at, various muscle subcellular compartments. Depletion of the CAP-interacting protein Vinculin results in a marked reduction in CAP levels at MASs, and vinculin mutants partially phenocopy Drosophila CAP mutants. These results show that CAP regulates junctional membrane and cytoskeletal organization at the membrane-cytoskeletal interface of stretch-sensitive structures, and they implicate integrin signaling through a CAP/Vinculin protein complex in stretch-sensitive organ assembly and function.
Details
- Title: Subtitle
- Cbl-associated protein regulates assembly and function of two tension-sensing structures in Drosophila
- Creators
- Rajnish Bharadwaj - Solomon H. Snyder Department of Neuroscience, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USAMadhuparna RoyTomoko OhyamaElena Sivan-LoukianovaMichael DelannoyThomas E LloydMarta ZlaticDaniel F EberlAlex L Kolodkin
- Resource Type
- Journal article
- Publication Details
- Development (Cambridge), Vol.140(3), pp.627-638
- Publisher
- England
- DOI
- 10.1242/dev.085100
- PMID
- 23293294
- PMCID
- PMC3561792
- ISSN
- 1477-9129
- eISSN
- 1477-9129
- Grant note
- R01 NS082563 / NINDS NIH HHS R01 NS035165 / NINDS NIH HHS R01 DC004848 / NIDCD NIH HHS Howard Hughes Medical Institute NS35165 / NINDS NIH HHS P30 DC010362 / NIDCD NIH HHS
- Language
- English
- Date published
- 02/01/2013
- Academic Unit
- Iowa Neuroscience Institute; Biology
- Record Identifier
- 9983992097702771
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