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J. Biol. Chem., Vol. 281, Issue 15, 9869-9881, April 14, 2006

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FEZ1 Dimerization and Interaction with Transcription Regulatory Proteins Involves Its Coiled-coil Region^*

Eliana M. Assmann¹, Marcos R. Alborghetti², Maria E. R. Camargo, and Jörg Kobarg³

From the Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, 13084-971 Campinas, SP and Universidade Estadual de Campinas, 13084-970 Campinas, SP, Brasil

The fasciculation and elongation protein 1 (FEZ1) is a mammalian orthologue of the Caenorhabditis elegans protein UNC-76, which is necessary for axon growth in that nematode. In previous studies FEZ1 has been found to interact with protein kinase C, DISC1, the agnoprotein of the human polyomavirus JC virus, and E4B, a U-box-type ubiquitin-protein isopeptide ligase. We reported previously that FEZ1 and its paralogue FEZ2 are proteins that interact with NEK1, a protein kinase involved in polycystic kidney disease and DNA repair mechanisms at the G₂/M phase of the cell cycle. Here we report the identification of 16 proteins that interact with human FEZ1-(221–396) in a yeast two-hybrid assay of a human fetal brain cDNA library. The 13 interacting proteins of known functions take part either in transcription regulation and chromatin remodeling (6 proteins), the regulation of neuronal cell development (2 proteins) and cellular transport mechanisms (3 proteins) or participate in apoptosis (2 proteins). We were able to confirm eight of the observed interactions by in vitro pull-down assays with recombinant fusion proteins. The confirmed interacting proteins include FEZ1 itself and three transcription controlling proteins (SAP30L, DRAP1, and BAF60a). In mapping studies we found that the C-terminal regions of FEZ1, and especially its coiled-coil region, are involved in its dimerization, its heterodimerization with FEZ2, and in the interaction with 10 of the identified interacting proteins. Our results give further support to the previous speculation of the functional involvement of FEZ1 in neuronal development but suggest further that FEZ1 may also be involved in transcriptional control.

Received for publication, December 13, 2005 , and in revised form, February 15, 2006.

^* This work was supported in part by the Fundação de Amparo à Pesquisa do Estado São Paulo through projects SmolbNet, CEPID, 05/00235-1, by the Conselho Nacional de Pesquisa e Desenvolvimento, and by Laboratório Nacional de Luz Síncrotron. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by postdoctoral fellowship from the Fundação de Amparo à Pesquisa do Estado São Paulo.

² Supported by a fellowship from the Fundação de Amparo à Pesquisa do Estado São Paulo.

³ To whom correspondence should be addressed: Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, Rua Giuseppe Máximo Scolfaro 10.000, C.P. 6192, 13084-971 Campinas, SP, Brasil. Tel.: 55-19-3512-1125; Fax: 55-19-3512-1006; E-mail: jkobarg{at}lnls.br.

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