Open Conformation of Ezrin Bound to Phosphatidylinositol 4,5-Bisphosphate and to F-actin Revealed by Neutron Scattering
作者： Jayant James Jayasundar , Jeong Ho Ju , Lilin He , Dazhi Liu , Flora Meilleur
关键词:
摘要: Ezrin is a member of the ezrin-radixin-moesin family (ERM) adapter proteins that are localized at interface between cell membrane and cortical actin cytoskeleton, they regulate variety cellular functions. The structure representing dormant closed conformation an ERM protein has previously been determined by x-ray crystallography. Here, using contrast variation small angle neutron scattering, we reveal structural changes full-length ezrin upon binding to signaling lipid phosphatidylinositol 4,5-bisphosphate (PIP2) F-actin. F-actin requires simultaneous PIP2. Once bound F-actin, opened forms more extensive contacts with than generally depicted, suggesting possible role in regulating interfacial dynamics underlying cytoskeleton. In addition, gel filtration, find conformational opening response PIP2 cooperative, but cooperativity disrupted phospho-mimic mutation S249D 4.1-ezrin/radixin/moesin (FERM) domain ezrin. Using surface plasmon resonance, show weakens affinity kinetics 4.1-ERM binding. study provides first view activated
sci-hub.se 参考文章(94)
Zimei Bu, David J.E. Callaway, Proteins move! Protein dynamics and long-range allostery in cell signaling. Advances in Protein Chemistry. ,vol. 83, pp. 163- 221 ,(2011) , 10.1016/B978-0-12-381262-9.00005-7
Andrea I. McClatchey, Merlin and ERM proteins: unappreciated roles in cancer development? Nature Reviews Cancer. ,vol. 3, pp. 877- 883 ,(2003) , 10.1038/NRC1213
Glatter O, Kratky O, Pilz I, Small Angle X-Ray Scattering ,(1982)
Nobuhiro Morone, Takahiro Fujiwara, Kotono Murase, Rinshi S. Kasai, Hiroshi Ike, Shigeki Yuasa, Jiro Usukura, Akihiro Kusumi, Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. Journal of Cell Biology. ,vol. 174, pp. 851- 862 ,(2006) , 10.1083/JCB.200606007
Fernando Martin-Belmonte, Ama Gassama, Anirban Datta, Wei Yu, Ursula Rescher, Volker Gerke, Keith Mostov, PTEN-Mediated Apical Segregation of Phosphoinositides Controls Epithelial Morphogenesis through Cdc42 Cell. ,vol. 128, pp. 383- 397 ,(2007) , 10.1016/J.CELL.2006.11.051
K Pestonjamasp, M R Amieva, C P Strassel, W M Nauseef, H Furthmayr, E J Luna, Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes. Molecular Biology of the Cell. ,vol. 6, pp. 247- 259 ,(1995) , 10.1091/MBC.6.3.247
G. D. Wignall, F. S. Bates, Absolute calibration of small-angle neutron scattering data Journal of Applied Crystallography. ,vol. 20, pp. 28- 40 ,(1987) , 10.1107/S0021889887087181
Richard F Lamb, Bradford W Ozanne, Christian Roy, Lynn McGarry, Christopher Stipp, Paul Mangeat, Daniel G Jay, Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts Current Biology. ,vol. 7, pp. 682- 688 ,(1997) , 10.1016/S0960-9822(06)00295-8
Jianquan Li, David J.E. Callaway, Zimei Bu, Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1. Journal of Molecular Biology. ,vol. 392, pp. 166- 180 ,(2009) , 10.1016/J.JMB.2009.07.005
Ichiko Saotome, Marcello Curto, Andrea I McClatchey, Ezrin is essential for epithelial organization and villus morphogenesis in the developing intestine. Developmental Cell. ,vol. 6, pp. 855- 864 ,(2004) , 10.1016/J.DEVCEL.2004.05.007