Neurofibromatosis type 2 protein co-localizes with elements of the cytoskeleton

Mcihael A. den Bakker, Metin Tascilar, Peter H.J. Riegman, Arnold C.P. Hekman, Wim Boersma, Patrick J.A. Janssen, Ton A.W. De Jong, Wiljan Hendriks, Theo H. Van der Kwast, Ellen C. Zwarthoff*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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The product of the neurofibromatosis type 2 (NF2) tumor suppressor gene is a 595-amino-acid protein bearing resemblance to a family of band-4.1-related proteins. These proteins, including ezrin, radixin, and moesin, probably function as molecular linking proteins, connecting the cytoskeleton to the cell membrane. On the grounds of the homology to the ezrin, radixin, and moesin proteins and on the basis of its predicted secondary structure, the NF2 protein is also thought to act as a cytoskeleton-cell membrane linking protein. Using monoclonal antibodies to amino- and carboxyl-terminal synthetic NF2 peptides we demonstrate the co-localization of the NF2 protein with elements of the cytoskeleton in a COS cell model system and in cultured human cells. Furthermore, the presence of the NF2 protein in tissue sections is shown. The monoclonal antibodies specifically stain smooth muscle cells and the stratum granulosum of the human epidermis. In cultured smooth muscle cells the NF2 protein co-localizes with actin stress fibers. Immunoelectron microscopy demonstrates the presence of the NF2 protein associated with keratohyalin granules and to a lesser extent with intermediate filaments in the human epidermis. We conclude that the NF2 protein is indeed associated with multiple elements of the cytoskeleton.

Original languageEnglish
Pages (from-to)1339-1349
Number of pages11
JournalAmerican Journal of Pathology
Issue number5
Publication statusPublished - Nov 1995


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