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Vol. 17, Issue 2, 886-894, February 2006

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Hsp27 Enhances Recovery of Splicing as well as Rephosphorylation of SRp38 after Heat Shock

Laura Marin-Vinader ^*, Chanseok Shin  , Carla Onnekink ^*, James L. Manley , and Nicolette H. Lubsen ^*

^* Department of Biochemistry, Radboud University Nijmegen, 6500 HB Nijmegen, The Netherlands; Department of Biological Sciences, Columbia University, New York, NY 10027

Submitted July 5, 2005; Revised November 9, 2005; Accepted November 30, 2005
Monitoring Editor: Greg Matera

A heat stress causes a rapid inhibition of splicing. Exogenous expression of Hsp27 did not prevent that inhibition but enhanced the recovery of splicing afterward. Another small heat shock protein, B-crystallin, had no effect. Hsp27, but not B-crystallin, also hastened rephosphorylation of SRp38—dephosphorylated a potent inhibitor of splicing—after a heat shock, although it did not prevent dephosphorylation by a heat shock. The effect of Hsp27 on rephosphorylation of SRp38 required phosphorylatable Hsp27. A Hsp90 client protein was required for the effect of Hsp27 on recovery of spicing and on rephosphorylation of SRp38. Raising the Hsp70 level by either a pre-heat shock or by exogenous expression had no effect on either dephosphorylation of SRp38 during heat shock or rephosphorylation after heat shock. The phosphatase inhibitor calyculin A prevented dephosphorylation of SRp38 during a heat shock and caused complete rephosphorylation of SRp38 after a heat shock, indicating that cells recovering from a heat shock are not deficient in kinase activity. Together our data show that the activity of Hsp27 in restoring splicing is not due to a general thermoprotective effect of Hsp27, but that Hsp27 is an active participant in the (de)phosphorylation cascade controlling the activity of the splicing regulator SRp38.

Present address: Whitehead Institute for Biomedical Research, MIT, Cambridge, MA 02142.

Address correspondence to: Nicolette H. Lubsen (N.Lubsen{at}science.ru.nl).

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