The NF2 tumor suppressor merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function

Nitasha Manchanda, Anna Lyubimova, Hsin-Yi Henry Ho, Marianne F. James, James F. Gusella, Narayanaswamy Ramesh, Scott B. Snapper, Vijaya Ramesh

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

The function of the NF2 tumor suppressor merlin has remained elusive despite increasing evidence for its role in actin cytoskeleton reorganization. The closely related ERM proteins (ezrin, radixin, and moesin) act as linkers between the cell membrane and cytoskeleton, and have also been implicated as active actin reorganizers. We report here that merlin and the ERMs can interact with and regulate N-WASP, a critical regulator of actin dynamics. Merlin and moesin were found to inhibit N-WASP-mediated actin assembly in vitro, a function that appears independent of their ability to bind actin. Furthermore, exogenous expression of a constitutively active ERM inhibits N-WASP-dependent Shigella tail formation, suggesting that the ERMs may function as inhibitors of N-WASP function in vivo. This novel function of merlin and the ERMs illustrates a mechanism by which these proteins directly exert their effects on actin reorganization and also provides new insight into N-WASP regulation.

Original languageEnglish (US)
Pages (from-to)12517-12522
Number of pages6
JournalJournal of Biological Chemistry
Volume280
Issue number13
DOIs
StatePublished - Apr 1 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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    Manchanda, N., Lyubimova, A., Ho, H-Y. H., James, M. F., Gusella, J. F., Ramesh, N., Snapper, S. B., & Ramesh, V. (2005). The NF2 tumor suppressor merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function. Journal of Biological Chemistry, 280(13), 12517-12522. https://doi.org/10.1074/jbc.C400583200