TY - JOUR
T1 - Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering
AU - Jayasundar, Jayant James
AU - Ju, Jeong Ho
AU - He, Lilin
AU - Liu, Dazhi
AU - Meilleur, Flora
AU - Zhao, Jinkui
AU - Callaway, David J.E.
AU - Bu, Zimei
PY - 2012/10/26
Y1 - 2012/10/26
N2 - Background: The structure of activated ezrin is not known. Results: We have determined the conformation of activated ezrin upon binding to PIP2 and to F-actin. Conclusion: Activated ezrin forms more extensive contacts with F-actin than generally depicted. Significance: This study provides new insight into the mechanisms by which ezrin assembles signaling complexes at the membrane-cytoskeleton interface.
AB - Background: The structure of activated ezrin is not known. Results: We have determined the conformation of activated ezrin upon binding to PIP2 and to F-actin. Conclusion: Activated ezrin forms more extensive contacts with F-actin than generally depicted. Significance: This study provides new insight into the mechanisms by which ezrin assembles signaling complexes at the membrane-cytoskeleton interface.
UR - http://www.scopus.com/inward/record.url?scp=84868262769&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.380972
DO - 10.1074/jbc.M112.380972
M3 - Article
C2 - 22927432
AN - SCOPUS:84868262769
SN - 0021-9258
VL - 287
SP - 37119
EP - 37133
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 44
ER -