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Multivalent Interactions with Fbw7 and Pin1 Facilitate Recognition of c-Jun by the SCFFbw7 Ubiquitin Ligase
Hospital Sick Children, Canada; University of British Columbia, Canada.
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, Faculty of Science & Engineering.
Hospital Sick Children, Canada.
University of Montreal, Canada.
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2018 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 26, no 1, p. 28-+Article in journal (Refereed) Published
Abstract [en]

Many regulatory proteins, including the transcription factor c-Jun, are highly enriched in disordered protein regions that govern growth, division, survival, differentiation, and response to signals. The stability of c-Jun is controlled by poorly understood regulatory interactions of its disordered region with both the E3 ubiquitin ligase SCFFbw7 and prolyl cis-trans isomerase Pin1. We use nuclear magnetic resonance and fluorescence studies of c-Jun to demonstrate that multisite c-Jun phosphorylation is required for high-affinity interaction with Fbw7. We show that the Pin1 WW and PPIase domains interact in a dynamic complex with multiply phosphorylated c-Jun. Importantly, Pin1 isomerizes a pSer-Pro peptide bond at the c-Jun N terminus that affects binding to Fbw7 and thus modulates the ubiquitin-mediated degradation of c-Jun. Our findings support the general principle that multiple weak binding motifs within disordered regions can synergize to yield high-affinity interactions and provide rapidly evolvable means to build and fine-tune regulatory events.

Place, publisher, year, edition, pages
CELL PRESS , 2018. Vol. 26, no 1, p. 28-+
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-144441DOI: 10.1016/j.str.2017.11.003ISI: 000419101700006PubMedID: 29225075OAI: oai:DiVA.org:liu-144441DiVA, id: diva2:1176701
Note

Funding Agencies|Canadian Institutes of Health Research [MOP-126129, MOP-114985]; Canadian Cancer Society Research Institute [703906, 703477]; Swedish Research Council; Swedish Cancer; Child Cancer Foundation; Carl Trygger Foundation; STINT (Swedish Foundation for International Cooperation in Research and Higher Education); Canada Research Chair in Intrinsically Disordered Proteins

Available from: 2018-01-23 Created: 2018-01-23 Last updated: 2018-01-23

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