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Volume 272, Number 34, Issue of August 22, 1997 pp. 21274-21280
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Protein Kinase C-mediated Interphase Lamin B Phosphorylation and Solubilization

(Received for publication, March 10, 1997, and in revised form, May 16, 1997)

Philippe Collas , Larry Thompson ^¶ , Alan P. Fields ^¶ , Dominic L. Poccia ^** and Jean-Claude Courvalin

From the  Department of Biochemistry, Norwegian College of Veterinary Medicine, 0033 Oslo, Norway, the ^¶ Sealy Center for Oncology, University of Texas Medical Branch, Galveston, Texas 77555, the ^** Department of Biology, Amherst College, Amherst, Massachusetts 01002, and the  Institut Jacques Monod, CNRS, Université Paris VII, 75251 Paris Cedex 5, France

Disassembly of the sperm nuclear envelope at fertilization is one of the earliest events in the development of the male pronucleus. We report that nuclear lamina disassembly in interphase sea urchin egg cytosol is a result of lamin B phosphorylation mediated by protein kinase C (PKC). Lamin B of permeabilized sea urchin sperm nuclei incubated in fertilized egg G₁ phase cytosolic extract is phosphorylated within 1 min of incubation and solubilized prior to sperm chromatin decondensation. Phosphorylation is Ca²⁺-dependent. It is reversibly inhibited by the PKC-specific inhibitor chelerythrine, a PKC pseudosubstrate inhibitor peptide, and a PKC substrate peptide, but not by inhibitors of PKA, p34^cdc2 or calmodulin kinase II. Phosphorylation is inhibited by immunodepletion of cytosolic PKC and restored by addition of purified rat brain PKC. Sperm lamin B is a substrate for rat brain PKC in vitro, resulting in lamin B solubilization. Two-dimensional phosphopeptide maps of lamin B phosphorylated by the cytosolic kinase and by purified rat PKC are virtually identical. These data suggest that PKC is the major kinase required for interphase disassembly of the sperm lamina.

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