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J. Biol. Chem., Vol. 280, Issue 23, 22060-22069, June 10, 2005

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Nuclear Translocation of Phospholipase C-₁ Is Linked to the Cell Cycle and Nuclear Phosphatidylinositol 4,5-Bisphosphate^*

Jonathan D. Stallings, Edward G. Tall, Srinivas Pentyala, and Mario J. Rebecchi

From the Department of Anesthesiology, State University of New York, Stony Brook, New York 11794

Nuclear phosphoinositides, especially phosphatidylinositol 4,5-bisphosphate, fluctuate throughout the cell cycle and are linked to proliferation and differentiation. Here we report that phospholipase C-₁ accumulates in the nucleus at the G₁/S boundary and in G₀ phases of the cell cycle. Furthermore, as wild-type protein accumulated in the nucleus, nuclear phosphatidylinositol 4,5-bisphosphate levels were elevated 3–5-fold, whereas total levels were decreased compared with asynchronous cultures. To test whether phosphatidylinositol 4,5-bisphosphate binding is important during this process, we introduced a R40D point mutation within the pleckstrin homology domain of phospholipase C-₁, which disables high affinity phosphatidylinositol 4,5-bisphosphate binding, and found that nuclear translocation was significantly reduced at G₁/S and in G₀. These results demonstrate a cell cycle-dependent compartmentalization of phospholipase C-₁ and support the idea that relative levels of phosphoinositides modulate the portioning of phosphoinositide-binding proteins between the nucleus and other compartments.

Received for publication, December 8, 2004 , and in revised form, March 31, 2005.

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

To whom correspondence should be addressed: Dept. of Anesthesiology, Health Sciences Center, Level 4, Rm. 076, State University of New York, Stony Brook, NY 11794-8480. Tel.: 631-444-8178; Fax: 631-444-2907; E-mail: mrebecchi{at}notes.cc.sunysb.edu.

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