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MBC in Press, published online ahead of print July 21, 2004
Mol. Biol. Cell 10.1091/mbc.E04-03-0234

A more recent version of this article appeared on October 1, 2004
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Submitted on March 18, 2004
Revised on June 16, 2004
Accepted on July 7, 2004

A Novel Mechanism for MAPK Localization

Eric Bind, Yelena Kleyner, Dorota Skowronska-Krawczyk, Emily Bien, Brian David Dynlacht, and Irma Sánchez*

Department of Pathology, New York University School of Medicine, New York, NY 10016

Monitoring Editor: Benjamin Glick

MAPKs/ERKs are typically thought to be soluble cytoplasmic enzymes that translocate to the nucleus subsequent to their phosphorylation by their activating kinases or MEKs. We report here the first example of nuclear translocation of a MAPK that occurs via temporally regulated exit from a membranous organelle. Confocal microscopy examining the subcellular localization of the ERK3 in several cell lines indicated that this enzyme was targeted to the Golgi/ERGIC. Deletion analysis of GFP-ERK3 uncovered a nuclear form that was carboxy-terminally truncated and established a Golgi targeting motif at the carboxy terminus. Immunoblot analysis of cells treated with the proteasome inhibitor MG132 further revealed two cleavage products suggesting that in vivo, carboxyterminal cleavage of the full length protein controls its subcellular localization. In support of this hypothesis, we found that deletion of a small region rich in acidic residues within the carboxy- terminus eliminated both the cleavage and nuclear translocation of GFP- ERK3. Finally, cell cycle synchronization studies revealed that the subcellular localization of ERK3 is temporally regulated. These data suggest a novel mechanism for the localization of a MAP kinase family member, ERK3, in which cell cycle regulated, site-specific proteolysis generates the nuclear form of the protein.

*Corresponding author. E-mail: irma.sanchez{at}med.nyu.edu






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