Cooperative stabilisation of 14-3-3σ protein–protein interactions via covalent protein modification-Reference-Cited by-同舟云学术

Cooperative stabilisation of 14-3-3σ protein–protein interactions via covalent protein modification

Published:2021 Issue:39 Volume:12 Page:12985-12992
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Falcicchio Marta¹²^ORCID,Ward Jake A.¹³,Chothia Sara Y.¹²^ORCID,Basran Jaswir⁴,Mohindra Alisha¹²^ORCID,Macip Salvador³⁵,Roversi Pietro¹⁴⁶^ORCID,Doveston Richard G.¹²^ORCID

Affiliation:

1. Leicester Institute for Structural and Chemical Biology, University of Leicester, University Road, Leicester, LE1 7RH, UK

2. School of Chemistry, University of Leicester, University Road, Leicester, LE1 7RH, UK

3. Mechanisms of Cancer and Aging Laboratory, Department of Molecular and Cell Biology, University of Leicester, University Road, Leicester, LE1 7RH, UK

4. Department of Molecular and Cell Biology, University of Leicester, University Road, Leicester, LE1 7RH, UK

5. FoodLab, Faculty of Health Sciences, Universitat Oberta de Catalunya, Barcelona, Spain

6. Institute of Agricultural Biology and Biotechnology, IBBA-CNR Unit of Milano, Via Bassini 15, I-20133, Milan, Italy

Abstract

The aminothiol WR-1065 covalently modifies 14-3-3σ to stabilse its interactions with p53 and ERα. It enhances the effect of fusicoccin A via a cooperative mechanism that leads to 14-3-3 partner-protein specific activty against cancer cells.

Funder

Royal Society

Wellcome Trust

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/SC/D1SC02120F

Reference30 articles.

1. Modulators of 14-3-3 Protein–Protein Interactions

2. Bioinformatic and experimental survey of 14-3-3-binding sites