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First published online 6 February 2007
doi: 10.1242/jcs.03390

Journal of Cell Science 120, 737-747 (2007)
Published by The Company of Biologists 2007
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Research Article

LAP2{alpha}-binding protein LINT-25 is a novel chromatin-associated protein involved in cell cycle exit

Nana Naetar1, Sabine Hutter1, Daniela Dorner1, Thomas Dechat1, Barbara Korbei1, Josef Gotzmann1, Hartmut Beug2 and Roland Foisner1,*

1 Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohr-Gasse 9, Vienna Biocenter, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria
2 Institute of Molecular Pathology, Vienna Biocenter, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria

* Author for correspondence (e-mail: roland.foisner{at}meduniwien.ac.at)

Accepted 4 January 2007

Lamina-associated polypeptide 2{alpha} (LAP2{alpha}) is a nuclear protein dynamically associating with chromatin during the cell cycle. In addition, LAP2{alpha} interacts with A-type lamins and retinoblastoma protein and regulates cell cycle progression via the E2F-Rb pathway. Using yeast two-hybrid analysis and three independent in vitro binding assays we identified a new LAP2{alpha} interaction partner of hitherto unknown functions, which we termed LINT-25. LINT-25 protein levels were upregulated during G1 phase in proliferating cells and upon cell cycle exit in quiescence, senescence and differentiation. Upon cell cycle exit LINT-25 accumulated in heterochromatin foci, and LAP2{alpha} protein levels were downregulated by proteasomal degradation. Although LAP2{alpha} was not required for the upregulation and reorganization of LINT-25 during cell cycle exit, transient expression of LINT-25 in proliferating cells caused loss of LAP2{alpha} and subsequent cell death. Our data show a role of LINT-25 and LAP2{alpha} during cell cycle exit, in which LINT-25 acts upstream of LAP2{alpha}.

Key words: Cell cycle, Chromatin, Differentiation, Lamins, Quiescence, Senescence


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