ErbB1 dimerization is promoted by domain co-confinement and stabilized by ligand binding-Reference-Cited by-同舟云学术

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ErbB1 dimerization is promoted by domain co-confinement and stabilized by ligand binding

Published:2011-10-23 Issue:11 Volume:18 Page:1244-1249
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Low-Nam Shalini T,Lidke Keith A,Cutler Patrick J,Roovers Rob C,van Bergen en Henegouwen Paul M P,Wilson Bridget S,Lidke Diane S

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2135.pdf

Reference42 articles.

1. Schlessinger, J. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110, 669–672 (2002).

2. Ferguson, K.M. et al. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol. Cell 11, 507–517 (2003).

3. Alvarado, D., Klein, D.E. & Lemmon, M.A. Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell 142, 568–579 (2010).

4. Chung, I. et al. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464, 783–787 (2010).

5. Clayton, A.H. et al. Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis. J. Biol. Chem. 280, 30392–30399 (2005).

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