CAV3:TRIM72:DYSF binds ANXAs

Stable Identifier
R-HSA-5263628
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

Mechanical stress and repetitive muscle contraction often causes membrane disruption to the sarcolemma. Healthy muscle is able to repair these disruptions by a Ca2+-dependent pathway. The combination of dysferlin (DYSF), caveolin 3 (CAV3) and tripartite motif-containing protein 72 (TRIM72 aka MG53) appears to be essential for the repair of muscle membrane damage (Cai et al. 2009). DYSF subsequently binds annexin A6 (ANXA6), a member of a family of phospholipid-binding proteins in a Ca2+-dependent manner. This interaction has been demonstrated in imaging experiments in zebrafish (Roostalu U & Strahle 2012). This interaction creates a platform for interacting proteins at the sarcolemma membrane surface and sequential recruitment of annexin A1 and A2 (ANXA1 and 2) to the repair site. The human event is deduced on the basis of experiments performed in mice (Lennon et al. 2003).

Literature References
PubMed ID Title Journal Year
14506282 Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing

Lennon, NJ, Kho, A, Bacskai, BJ, Perlmutter, SL, Hyman, BT, Brown, RH

J. Biol. Chem. 2003
22421042 In vivo imaging of molecular interactions at damaged sarcolemma

Roostalu, U, Strähle, U

Dev. Cell 2012
19380584 Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin

Cai, C, Weisleder, N, Ko, JK, Komazaki, S, Sunada, Y, Nishi, M, Takeshima, H, Ma, J

J. Biol. Chem. 2009
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