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J Biol Chem, Vol. 273, Issue 10, 5892-5902, March 6, 1998
From the Center for Gerontology, Allegheny University of the Health
Sciences and the Division of Rheumatology, Department of Medicine,
University of Pennsylvania, Philadelphia, Pennsylvania 19104
Activating transcription factor
2 (ATF2) is regulated by phosphorylation via the Jun N-terminal kinase,
and its binding activity is markedly induced at late stages of T and B
lymphocyte activation (Feuerstein, N., Firestein, R., Aiyer, N.,
Xiao, H., Murasko, D., and Cristofalo, V. (1996)
J. Immunol. 156, 4582-4593). To identify proteins
that interact specifically with ATF2 in lymphocytes, the yeast
two-hybrid interaction system was employed using ATF2 cDNA as a
"bait." In two separate screenings, a clone was identified that
revealed a novel sequence with homology to several members of the
ubiquitin-conjugating enzyme family. An identical sequence was recently
reported as the human homolog of the yeast UBC9, hUBC9. Northern blot
analysis revealed a 1.3-kilobase RNA transcript, which showed
differential levels of expression in various human tissues and a
moderate induction after a 48-h stimulation of peripheral blood T
lymphocytes. An antibody that was generated against the bacterially
expressed glutathione S-transferase-hUBC9 detected a
~19-kDa protein, which localizes predominantly in the nuclei of T
cells. Further quantitative assays using the yeast two-hybrid system
confirmed a high and specific level of interaction of hUBC9 with ATF2
and lack of interaction with lamin or control vectors. Two other cyclic
AMP-responsive element-binding transcription factors, CREB and ATF1,
also showed significant levels of interaction with hUBC9. However, this
interaction was severalfold lower as compared with ATF2. Far Western
blot analysis confirmed the specific binding of ATF2 and hUBC9 also
in vitro. Evidence is presented that indicates a
physiological significance for the interaction of hUBC9 with ATF2.
(a) We show that ATF2 is ubiquitinated in vivo
and in vitro, and (b) ATF2 ubiquitination
in vitro is facilitated by addition of purified hUBC9.
(c) ATF2 is shown to undergo a proteolytic process, which
is rapidly regulated upon T cell activation concomitant with induction
of ATF2 phosphorylation. (d) A proteasome inhibitor delays
the down-regulation of ATF2 phophorylation after T cell activation.
Taken collectively, these results implicate a role for hUBC9 and the
ubiquitin/proteasome pathway in regulation of ATF2 in T cells.
Association of Activating Transcription Factor 2 (ATF2) with the
Ubiquitin-conjugating Enzyme hUBC9
IMPLICATION OF THE UBIQUITIN/PROTEASOME PATHWAY IN REGULATION OF
ATF2 IN T CELLS
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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