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First published online August 29, 2005
doi: 10.1242/10.1242/jcs.02521

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The nuclear-envelope protein and transcriptional repressor LAP2ß interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation

Raz Somech^1,2,3,*, Sigal Shaklai^1,2,*, Orit Geller^1,2, Ninette Amariglio^1,2, Amos J. Simon^1,2, Gideon Rechavi^1,2, and Einav Nili Gal-Yam^1,2

¹ Sheba Cancer Research Center and the Institute of Hematology, The Chaim Sheba Medical Center, Tel-Hashomer 52621, Israel
² Sackler School of Medicine, Tel-Aviv University, Tel-Hashomer 52621, Israel
³ Dana Children's Hospital, Tel Aviv Sourasky Medical Center, Israel

Author for correspondence (e-mail: gidi.rechavi{at}sheba.health.gov.il)

Accepted 6 June 2005

Nuclear-envelope proteins have been implicated in diverse and fundamental cell functions, among them transcriptional regulation. Gene expression at the territory of the nuclear periphery is known to be repressed by epigenetic modifications such as histone deacetylation and methylation. However, the mechanism by which nuclear-envelope proteins are involved in such modifications is still obscure. We have previously shown that LAP2ß, an integral nuclear-envelope protein that contains the chromatin-binding LEM domain, was able to repress the transcriptional activity of the E2F5-DP3 heterodimer. Here, we show that LAP2ß's repressive activity is more general, encompassing various E2F members as well as other transcription factors such as p53 and NF-B. We further show that LAP2ß interacts at the nuclear envelope with HDAC3, a class-I histone deacetylase, and that TSA (an HDAC inhibitor) abrogates LAP2ß's repressive activity. Finally, we show that LAP2ß is capable of inducing histone-H4 deacetylation. Our data provide evidence for the existence of a previously unknown repressive complex, composed of an integral nuclear membrane protein and a histone modifier, at the nuclear periphery.

Key words: HDAC3, LAP2ß, Histone modification, Nuclear envelope, Transcriptional repression, Chromatin architecture

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