Document Detail


Cbl-associated protein regulates assembly and function of two tension-sensing structures in Drosophila.
MedLine Citation:
PMID:  23293294     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Rajnish Bharadwaj; Madhuparna Roy; Tomoko Ohyama; Elena Sivan-Loukianova; Michael Delannoy; Thomas E Lloyd; Marta Zlatic; Daniel F Eberl; Alex L Kolodkin
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Development (Cambridge, England)     Volume:  140     ISSN:  1477-9129     ISO Abbreviation:  Development     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-07     Completed Date:  2013-03-07     Revised Date:  2013-08-09    
Medline Journal Info:
Nlm Unique ID:  8701744     Medline TA:  Development     Country:  England    
Other Details:
Languages:  eng     Pagination:  627-38     Citation Subset:  IM    
Affiliation:
Solomon H. Snyder Department of Neuroscience, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
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MeSH Terms
Descriptor/Qualifier:
Actin Cytoskeleton / metabolism,  physiology
Amino Acid Sequence
Animal Structures / metabolism,  physiology*,  ultrastructure
Animals
Binding Sites
Cell Membrane / metabolism,  physiology
Cell-Matrix Junctions / metabolism,  physiology
Cytoskeletal Proteins / genetics,  metabolism*
Drosophila / anatomy & histology,  genetics,  metabolism,  physiology*
Electrophysiological Phenomena
Gene Expression Regulation, Developmental*
Genome, Insect
Hearing Disorders / genetics,  pathology,  veterinary
Integrins / metabolism
Larva / genetics,  metabolism,  physiology,  ultrastructure
Mechanotransduction, Cellular
Microscopy, Electron, Transmission
Multiprotein Complexes / genetics,  metabolism
Muscles / cytology,  metabolism
Protein Interaction Mapping
Sequence Homology, Amino Acid
Signal Transduction
Talin / genetics,  metabolism
Vibration
Vinculin / genetics,  metabolism
src Homology Domains
Grant Support
ID/Acronym/Agency:
NS35165/NS/NINDS NIH HHS; P30 DC010362/DC/NIDCD NIH HHS; R01 DC004848/DC/NIDCD NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Cytoskeletal Proteins; 0/Integrins; 0/Multiprotein Complexes; 0/Talin; 125361-02-6/Vinculin
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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