Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export

Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export

CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214. Here,...

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Bibliographic Details
Main Authors: Sarah A. Port, Thomas Monecke, Achim Dickmanns, Christiane Spillner, Romina Hofele, Henning Urlaub, Ralf Ficner, Ralph H. Kehlenbach
Format: Article
Language:English
Published: Elsevier 2015-10-01
Series:Cell Reports
Online Access:http://www.sciencedirect.com/science/article/pii/S2211124715010670

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http://www.sciencedirect.com/science/article/pii/S2211124715010670

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