An actin-dependent annexin complex mediates plasma membrane repair in muscle

Alexis R. Demonbreun, Mattia Quattrocelli, David Y. Barefield, Madison V. Allen, Kaitlin E. Swanson, Elizabeth M. McNally*

*Corresponding author for this work

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

Disruption of the plasma membrane often accompanies cellular injury, and in muscle, plasma membrane resealing is essential for efficient recovery from injury. Muscle contraction, especially of lengthened muscle, disrupts the sarcolemma. To define the molecular machinery that directs repair, we applied laser wounding to live mammalian myofibers and assessed translocation of fluorescently tagged proteins using high-resolution microscopy. Within seconds of membrane disruption, annexins A1, A2, A5, and A6 formed a tight repair "cap." Actin was recruited to the site of damage, and annexin A6 cap formation was both actin dependent and Ca2+ regulated. Repair proteins, including dysferlin, EHD1, EHD2, MG53, and BIN1, localized adjacent to the repair cap in a "shoulder" region enriched with phosphatidlyserine. Dye influx into muscle fibers lacking both dysferlin and the related protein myoferlin was substantially greater than control or individual null muscle fibers, underscoring the importance of shoulder-localized proteins. These data define the cap and shoulder as subdomains within the repair complex accumulating distinct and nonoverlapping components.

Original languageEnglish (US)
Pages (from-to)705-718
Number of pages14
JournalJournal of Cell Biology
Volume213
Issue number6
DOIs
StatePublished - Jan 1 2016

ASJC Scopus subject areas

  • Cell Biology

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