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Vol. 12, Issue 6, 1811-1817, June 2001
and
*Department of Biological Sciences, Carnegie Mellon University,
Pittsburgh, Pennsylvania 15213; and The role of the mitogen-activated protein kinase kinase
(MKK)/extracellular-activated protein kinase (ERK) pathway in mitotic Golgi disassembly is controversial, in part because Golgi-localized targets have not been identified. We observed that Golgi reassembly stacking protein 55 (GRASP55) was phosphorylated in mitotic cells and
extracts, generating a mitosis-specific phospho-epitope recognized by
the MPM2 mAb. This phosphorylation was prevented by mutation of ERK
consensus sites in GRASP55. GRASP55 mitotic phosphorylation was
significantly reduced, both in vitro and in vivo, by treatment with
U0126, a potent and specific inhibitor of MKK and thus ERK activation.
Furthermore, ERK2 directly phosphorylated GRASP55 on the same residues
that generated the MPM2 phospho-epitope. These results are the first
demonstration of GRASP55 mitotic phosphorylation and indicate that the
MKK/ERK pathway directly phosphorylates the Golgi during mitosis.
Department of
Chemistry and Biochemistry and Howard Hughes Medical Institute,
University of Colorado, Boulder, Colorado 80309
Corresponding author. E-mail address:
linstedt{at}andrew.cmu.edu.
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