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

Federica Sotgia, Jean Kyung Lee, Kallol Das, Mark Bedford, Tamara C. Petrucci, Pompeo Macioce, Massimo Sargiacomo, Franca Dagna Bricarelli, Carlo Minetti, Marius Sudol, Michael P. Lisantia

Research output: Contribution to journalArticle

Abstract

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 β-dystroglycan, an integral membrane component of the dystrophin complex. Our results indicare that caveolin-3 co-localizes, co-fractionates, and coimmunoprecipitates with a fusion protein containing the cytoplasmic tail of β-dystroglycan. In addition, we show that a novel WW-llke domain within caveolin-3 directly recognizes the extreme C terminus of β-dystroglycan that contains a PPXY motif. As the WW domain of dystrophin recognizes the same site within β-dystroglycan, we also demonstrate that caveolin-3 can effectively block the interaction of dystrophin with β-dystroglycan. In this regard, interaction of caveolin-3 with β-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.

Original languageEnglish
Pages (from-to)38048-38058
Number of pages11
JournalJournal of Biological Chemistry
Volume275
Issue number48
DOIs
Publication statusPublished - Dec 1 2000

ASJC Scopus subject areas

  • Biochemistry

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    Sotgia, F., Lee, J. K., Das, K., Bedford, M., Petrucci, T. C., Macioce, P., Sargiacomo, M., Bricarelli, F. D., Minetti, C., Sudol, M., & Lisantia, M. P. (2000). Caveolin-3 directly interacts with the C-terminal tail of β-dystroglycan. Identification of a central WW-like domain within caveolin family members. Journal of Biological Chemistry, 275(48), 38048-38058. https://doi.org/10.1074/jbc.M005321200