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Molecular and Cellular Biology, March 2000, p. 1699-1712, Vol. 20, No. 5
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Cloning and Characterization of SCHIP-1, a Novel Protein Interacting Specifically with Spliced Isoforms and Naturally Occurring Mutant NF2 Proteins

Laurence Goutebroze,1,2,* Estelle Brault,1,2 Christian Muchardt,3 Jacques Camonis,4 and Gilles Thomas1,2

U4341 and U248,4 INSERM-Institut Curie, 75005 Paris, CEPH Fondation Jean Dausset, 75010 Paris,2 and Unité des Virus Oncogènes, UA1644 CNRS, Département des Biotechnologies, Institut Pasteur, 75015 Paris,3 France

Received 28 May 1999/Returned for modification 3 August 1999/Accepted 15 November 1999

The neurofibromatosis type 2 (NF2) protein, known as schwannomin or merlin, is a tumor suppressor involved in NF2-associated and sporadic schwannomas and meningiomas. It is closely related to the ezrin-radixin-moesin family members, implicated in linking membrane proteins to the cytoskeleton. The molecular mechanism allowing schwannomin to function as a tumor suppressor is unknown. In attempt to shed light on schwannomin function, we have identified a novel coiled-coil protein, SCHIP-1, that specifically associates with schwannomin in vitro and in vivo. Within its coiled-coil region, this protein is homologous to human FEZ proteins and the related Caenorhabditis elegans gene product UNC-76. Immunofluorescent staining of transiently transfected cells shows a partial colocalization of SCHIP-1 and schwannomin, beneath the cytoplasmic membrane. Surprisingly, immunoprecipitation assays reveal that in a cellular context, association with SCHIP-1 can be observed only with some naturally occurring mutants of schwannomin, or a schwannomin spliced isoform lacking exons 2 and 3, but not with the schwannomin isoform exhibiting growth-suppressive activity. Our observations suggest that SCHIP-1 interaction with schwannomin is regulated by conformational changes in schwannomin, possibly induced by posttranslational modifications, alternative splicing, or mutations.

* Corresponding author. Mailing address: CEPH Fondation Jean Dausset, 27 rue Juliette Dodu, 75010 Paris, France. Phone: 33 1 53 72 51 20. Fax: 33 1 53 72 51 92. E-mail: goutebroze{at}cephb.fr.

Molecular and Cellular Biology, March 2000, p. 1699-1712, Vol. 20, No. 5
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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