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Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members.

Caveolin-3, the most recently recognized member of the caveolin gene family, is muscle-specific and is found in both cardiac and skeletal muscle, as well as smooth muscle cells. Several independent lines of evidence indicate that caveolin-3 is localized to the sarcolemma, where it associates with the dystrophin-glycoprotein complex. However, it remains unknown which component of the dystrophin complex interacts with caveolin-3. Here, we demonstrate that caveolin-3 directly interacts with beta-dystroglycan, an integral membrane component of the dystrophin complex. Our results indicate that caveolin-3 co-localizes, co-fractionates, and co-immunoprecipitates with a fusion protein containing the cytoplasmic tail of beta-dystroglycan. In addition, we show that a novel WW-like domain within caveolin-3 directly recognizes the extreme C terminus of beta-dystroglycan that contains a PPXY motif. As the WW domain of dystrophin recognizes the same site within beta-dystroglycan, we also demonstrate that caveolin-3 can effectively block the interaction of dystrophin with beta-dystroglycan. In this regard, interaction of caveolin-3 with beta-dystroglycan may competitively regulate the recruitment of dystrophin to the sarcolemma. We discuss the possible implications of our findings in the context of Duchenne muscular dystrophy.

Pubmed ID: 10988290

Authors

  • Sotgia F
  • Lee JK
  • Das K
  • Bedford M
  • Petrucci TC
  • Macioce P
  • Sargiacomo M
  • Bricarelli FD
  • Minetti C
  • Sudol M
  • Lisanti MP

Journal

The Journal of biological chemistry

Publication Data

December 1, 2000

Associated Grants

  • Agency: Telethon, Id: 1111

Mesh Terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Caveolin 3
  • Caveolins
  • Cytoskeletal Proteins
  • Dystroglycans
  • Membrane Glycoproteins
  • Mice
  • Molecular Sequence Data
  • Precipitin Tests
  • Protein Binding
  • Sequence Homology, Amino Acid