Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations.

Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations.

Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans.We determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell pol...

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Main Authors: Fumihiko Nakamura, Outi Heikkinen, Olli T Pentikäinen, Teresia M Osborn, Karen E Kasza, David A Weitz, Olga Kupiainen, Perttu Permi, Ilkka Kilpeläinen, Jari Ylänne, John H Hartwig, Thomas P Stossel
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2009-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2654154?pdf=render

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http://europepmc.org/articles/PMC2654154?pdf=render

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