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Volume 272, Number 51, Issue of December 19, 1997 pp. 32163-32168
(Received for publication, July 25, 1997, and in revised form, September 15, 1997)
,
From the Ruttenberg Cancer Center, Mount Sinai School of Medicine,
New York, New York 10029, the Regulatory proteins are often ubiquitinated,
depending on their phosphorylation status as well as on their
association with ancillary proteins that serve as adapters of the
ubiquitination machinery. We previously demonstrated that c-Jun is
targeted for ubiquitination by its association with inactive c-Jun
NH2-terminal kinase (JNK). Phosphorylation by
activated JNK protects c-Jun from ubiquitination, thus by prolonging
its half-life. In the study reported here, we determined the ability of
JNK to target ubiquitination of its other substrates (Elk1 and
activating transcription factor 2 (ATF2)) and associated proteins (ATF2
and JunB). We demonstrate that phosphorylation by JNK protects ATF2,
but not Elk1, from JNK-targeted ubiquitination. We also show that
association of inactive JNK with JunB or ATF2 is necessary to target
them for ubiquitination. Unlike its targeting of c-Jun, JNK requires
additional cellular components, yet to be identified, to target the
ubiquitination of ATF2. Elk1 is phosphorylated by JNK, but JNK neither
associates with nor targets Elk1 for ubiquitination. The implications
for the dual role of JNK in the regulation of ubiquitination and
stability of c-Jun, ATF2, and JunB in normally growing
versus stressed cells are discussed.
Department of Cell Biology
and Anatomy, New York Medical College, Valhalla, New York 10595, and
the § Howard Hughes Medical Institute, University of
Massachusetts Medical Center, Worcester, Masschusetts 01605
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