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Tumour suppression by merlin and 4.1 proteins

Members of the protein 4.1 superfamily are FERM-domain proteins that connect cell-surface glycoproteins with the actin cytoskeleton. The superfamily includes protein tyrosine phosphatases, 4.1 proteins, and ERM proteins such as ezrin and merlin/schwannomin — the protein inactivated in neurofibromatosis 2. In a Commentary on p. 3991, David Gutmann and co-workers review work showing that certain 4.1 and ERM proteins are tumour suppressors, highlighting recent studies that have provided insight into how they function. Loss of merlin is associated with development of schwannoma and meningioma; similarly, loss of protein 4.1B has been linked with a variety of tumors. Merlin is known to associate with cell surface molecules such as CD44 and appears to engage in intramolecular interactions that regulate its ability to interact with actin and other proteins. Gutmann and coworkers propose that signalling through Rho GTPases activates kinases that block these intramolecular interactions and thereby inhibit tumour suppression by merlin. Given the sequence similarity shared by merlin and the rest of this superfamily, other 4.1 tumour suppressors might act in the same way.

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Related articles in JCS:

Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation

Chun-Xiao Sun, Victoria A. Robb, and David H. Gutmann
JCS 2002 115: 3991-4000. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?