Journal
STRUCTURE
Volume 20, Issue 10, Pages 1737-1745Publisher
CELL PRESS
DOI: 10.1016/j.str.2012.08.004
Keywords
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Funding
- Canadian Institutes of Health Research [MOP-93520, MOP-89903]
- Ontario Ministry of Research and Innovation
- Canada Research Chairs Program
- Offices of Biological and Environmental Research
- Basic Energy Sciences of the U.S. Department of Energy
- National Center for Research Resources [P41RR012408]
- National Institute of General Medical Sciences [P41GM103473]
- National Institutes of Health
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Plasma membrane repair involves the coordinated effort of proteins and the inner phospholipid surface to mend the rupture and return the cell back to homeostasis. Here, we present the three-dimensional structure of a multiprotein complex that includes S100A10, annexin A2, and AHNAK, which along with dysferlin, functions in muscle and cardiac tissue repair. The 3.5 angstrom resolution X-ray structure shows that a single region from the AHNAK C terminus is recruited by an S100A10-annexin A2 heterotetramer, forming an asymmetric ternary complex. The AHNAK peptide adopts a coil conformation that arches across the heterotetramer contacting both annexin A2 and S100A10 protomers with tight affinity (similar to 30 nM) and establishing a structural rationale whereby both S100A10 and annexin proteins are needed in AHNAK recruitment. The structure evokes a model whereby AHNAK is targeted to the membrane surface through sandwiching of the binding region between the S100A10/annexin A2 complex and the phospholipid membrane.
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