Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Nov;30(6):438–448. doi: 10.1152/physiol.00019.2015

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

©2015 Int. Union Physiol. Sci./Am. Physiol. Soc.

PMC Copyright notice

FIGURE 3. — Proposed roles of MG53/TRIM72 in mediating membrane repair

MG53/TRIM72 interacts with phosphatidylserine in the plasma membrane in a complex containing dysferlin and Cav-3. MG53/TRIM72 and dysferlin close the membrane wound with vesicles. Vesicle transport is facilitated by myosin motor proteins. Cav-3 may regulate MG53/TRIM72-mediated membrane fusion and is enriched in caveolae or plasma membrane invaginations. PTRF may aid in the formation and stabilization of these caveolae by interaction with Cav-3 and MG53/TRIM72 through cholesterol. PTRF also binds and may help localize dysferlin.