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Vol. 16, No. 4, pp. 439-451, February 15, 2002
-TrCP ubiquitin ligase by hnRNP-U
1 The Lautenberg Center for Immunology, The Hebrew
University-Hadassah Medical School, Jerusalem 91120, Israel;
2 Protein Interaction Laboratory, University of Southern
Denmark, DK-5230 Odense M, Denmark; 3 Centre for Immunology,
St. Vincent's Hospital and University of New South Wales, Sydney 2010, Australia; 4 Signal Research Division, Celgene Corp., San
Diego, California 92121, USA
-TrCP/E3RS (E3RS) is the F-box protein that functions as the
receptor subunit of the SCF
-TrCP ubiquitin ligase (E3).
Surprisingly, although its two recognized substrates, I
B
and
-catenin, are present in the cytoplasm, we have found that E3RS is
located predominantly in the nucleus. Here we report the isolation of
the major E3RS-associated protein, hnRNP-U, an abundant nuclear
phosphoprotein. This protein occupies E3RS in a specific and
stoichiometric manner, stabilizes the E3 component, and is likely
responsible for its nuclear localization. hnRNP-U binding was abolished
by competition with a pIB peptide, or by a specific point
mutation in the E3RS WD region, indicating an E3-substrate-type
interaction. However, unlike pIB, which is targeted by
SCF-TrCP for degradation, the E3-bound hnRNP-U is stable
and is, therefore, a pseudosubstrate. Consequently, hnRNP-U engages a
highly neddylated active SCF-TrCP, which dissociates in
the presence of a high-affinity substrate, resulting in ubiquitination
of the latter. Our study points to a novel regulatory mechanism, which
secures the localization, stability, substrate binding threshold, and
efficacy of a specific protein-ubiquitin ligase.
[Key Words:
-TrCP/E3RS; hnRNP-U; IB; nuclear
transport; ubiquitin ligase]
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