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J Biol Chem, Vol. 275, Issue 17, 12363-12366, April 28, 2000

ACCELERATED PUBLICATION
ICln Is Essential for Cellular and Early Embryonic Viability*

William T. PuDagger , Kevin WickmanDagger §, and David E. Clapham

From the Cardiovascular Division, Howard Hughes Medical Institute, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115

pICln is a 26-kDa protein that is ubiquitously expressed and highly conserved from Xenopus laevis to Homo sapiens. The physiological functions of pICln remain to be established. To address this question, we disrupted the ICln gene in embryonic stem cells. We found that murine embryos lacking ICln die early in gestation (between stages E3.5 and E7.5). Furthermore, we found that ICln is essential for embryonic stem cell viability. Previously, we showed that pICln interacts directly with a homolog of a yeast protein that binds a PAK-like kinase and participates in the regulation of cell morphology and cell cycling. pICln also forms a complex with several core spliceosomal proteins, and this interaction may play a role in the regulation of spliceosomal biogenesis. Collectively, these data strongly suggest that pICln participates in critical cellular pathways, including regulation of the cell cycle and RNA processing.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger These authors contributed equally to this work.

§ Present address: Dept. of Pharmacology, University of Minnesota, 6-120 Jackson Hall, 321 Church St., S.E., Minneapolis, MN 55455.

To whom correspondence should be addressed: Howard Hughes Medical Institute, Children's Hospital, Harvard Medical School, 1309 Enders, 320 Longwood Ave., Boston, MA 02115. Tel.: 617-355-6163; Fax: 617-355-3692; E-mail: clapham@rascal.med.harvard.edu.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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