| First Author | Sotgia F | Year | 2000 |
| Journal | J Biol Chem | Volume | 275 |
| Issue | 48 | Pages | 38048-58 |
| PubMed ID | 10988290 | Mgi Jnum | J:66004 |
| Mgi Id | MGI:1927714 | Doi | 10.1074/jbc.M005321200 |
| Citation | Sotgia F, et al. (2000) Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. IDENTIFICATION OF A CENTRAL WW-LIKE DOMAIN WITHIN CAVEOLIN FAMILY MEMBERS. J Biol Chem 275(48):38048-58 |
| abstractText | 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. |
