DYSF, CAV3 and TRIM72 bind

Stable Identifier
R-HSA-5263633
Type
Reaction [binding]
Species
Homo sapiens
Compartment
cytoplasmic vesicle membrane, plasma membrane
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
DYSF, CAV3 and TRIM72 bind
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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). CAV3 probably acts as a scaffolding protein in caveolar membranes and can interact with DYSF (Matsuda et al. 2001), a surface membrane protein which promotes the fusion of intracellular vesicles with each other and with the sarcolemma at the site of injury. TRIM72 is required for transport of DYSF to the site of injury.
Literature References
PubMed ID Title Journal Year
11532985 The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle

Matsuda, C, Hayashi, YK, Ogawa, M, Aoki, M, Murayama, K, Nishino, I, Nonaka, I, Arahata, K, Brown, RH

Hum. Mol. Genet. 2001
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
Participants
Input
Output
Participates
as an event of
This event is regulated
Positively by
Regulator
Ca2+ [cytosol]
Authored
Jassal, B  (2014-02-12)
Reviewed
D'Eustachio, P  (2015-02-11)
Created
Jassal, B  (2014-02-12)
Cite Us!