QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Figures Only Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nili, E. Articles by Rechavi, G. Search for Related Content PubMed PubMed Citation Articles by Nili, E. Articles by Rechavi, G.

Nuclear membrane protein LAP2ß mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)

¹ Pediatric Hemato-Oncology Department, Division of Hematology, Chaim Sheba Medical Center, Tel-Hashomer and the Sackler School of Medicine, Tel-Aviv University, Israel
² Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot, Israel
³ National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, MD 21702, USA

*Author for correspondence (e-mail: amosimon{at}yahoo.com)

Accepted June 10, 2001

LAP2ß is an integral membrane protein of the nuclear envelope involved in chromatin and nuclear architecture. Using the yeast two-hybrid system, we have cloned a novel LAP2ß-binding protein, mGCL, which contains a BTB/POZ domain and is the mouse homologue of the Drosophila germ-cell-less (GCL) protein. In Drosophila embryos, GCL was shown to be essential for germ cell formation and was localized to the nuclear envelope. Here, we show that, in mammalian cells, GCL is co-localized with LAP2ß to the nuclear envelope. Nuclear fractionation studies reveal that mGCL acts as a nuclear matrix component and not as an integral protein of the nuclear envelope. Recently, mGCL was found to interact with the DP3 component of the E2F transcription factor. This interaction reduced the transcriptional activity of the E2F-DP heterodimer, probably by anchoring the complex to the nuclear envelope. We demonstrate here that LAP2ß is also capable of reducing the transcriptional activity of the E2F-DP complex and that it is more potent than mGCL in doing so. Co-expression of both LAP2ß and mGCL with the E2F-DP complex resulted in a reduced transcriptional activity equal to that exerted by the pRb protein.

Key words: GCL, Germ-cell-less, LAP2, Nuclear envelope, Thymopoietin, Transcription regulation

This article has been cited by other articles:

				T. Kimura, C. Ito, S. Watanabe, T. Takahashi, M. Ikawa, K. Yomogida, Y. Fujita, M. Ikeuchi, N. Asada, K. Matsumiya, et al. Mouse Germ Cell-Less as an Essential Component for Nuclear Integrity Mol. Cell. Biol., February 15, 2003; 23(4): 1304 - 1315. [Abstract] [Full Text] [PDF]

				R. D. Goldman, Y. Gruenbaum, R. D. Moir, D. K. Shumaker, and T. P. Spann Nuclear lamins: building blocks of nuclear architecture Genes & Dev., March 1, 2002; 16(5): 533 - 547. [Full Text] [PDF]

				Y. Gruenbaum, K. K. Lee, J. Liu, M. Cohen, and K. L. Wilson The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans J. Cell Sci., January 3, 2002; 115(5): 923 - 929. [Abstract] [Full Text] [PDF]

				T. P. Spann, A. E. Goldman, C. Wang, S. Huang, and R. D. Goldman Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription J. Cell Biol., February 18, 2002; 156(4): 603 - 608. [Abstract] [Full Text] [PDF]