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First published online February 21, 2007

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New LAP dog for nuclear lamins

The nuclear protein lamina-associated polypeptide 2 (LAP2) plays a key role in chromatin organisation, cell cycle regulation and differentiation. These functions are, in part, regulated by its interactions with the A-type lamins that reside in the nuclear compartment and the tumour suppressor pRb. To investigate the mechanisms of LAP2 function in chromatin organisation and cell cycle control, Nana Naetar and co-workers (p. 737) used a yeast two-hybrid approach to identify a novel LAP2 binding partner, LAP2-interactor-25 (LINT-25). The authors confirmed the direct interaction between LINT-25 and the LAP2 C-terminus with additional in vitro binding assays. LINT-25 protein is upregulated and relocalises to heterochromatin foci when cells exit the cell cycle, and its upregulation is tightly coupled with the downregulation and proteasomal degradation of LAP2. Furthermore, the authors demonstrate that LINT-25 upregulation is not dependent on LAP2 but that LINT-25 acts upstream of LAP2 to regulate its cell cycle function. The authors propose a model whereby LINT-25 causes loss of LAP2 by affecting its stability, thus contributing to the proper timing of cell cycle exit.

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Related articles in JCS:

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

Nana Naetar, Sabine Hutter, Daniela Dorner, Thomas Dechat, Barbara Korbei, Josef Gotzmann, Hartmut Beug, and Roland Foisner
JCS 2007 120: 737-747. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?