Interplay between SUMOylation and NEDDylation regulates RPL11 localization and function-Reference-Cited by-同舟云学术

Interplay between SUMOylation and NEDDylation regulates RPL11 localization and function

Published:2018-07-19 Issue:1 Volume:33 Page:643-651
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

El Motiam Ahmed¹,Vidal Santiago¹,De La Cruz-Herrera Carlos F.²³,Da Silva-Álvarez Sabela⁴,Baz-Martínez Maite¹,Seoane Rocío¹,Vidal Anxo¹,Rodríguez Manuel S.⁵⁶,Xirodimas Dimitris P.⁷,Carvalho Ana Sofia⁸,Beck Hans Christian⁹,Matthiesen Rune⁸,Collado Manuel⁴,Rivas Carmen¹²

Affiliation:

1. Centro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS)Universidade de Santiago de Compostela e Instituto de Investigaciones Sanitarias Santiago de Compostela Spain

2. Departamento de Biología Molecular y CelularCentro Nacional de Biotecnología–Consejo Superior de Investigaciones Científicas (CNB-CSIC) Madrid Spain

3. Department of Molecular GeneticsUniversity of Toronto Toronto Ontario Canada

4. Instituto de Investigatión Sanitaria de Santiago de CompostelaComplexo Hospitalario Universitario de Santiago de CompostelaServicio Gallego de Salud Santiago de Compostela Spain

5. Advanced Technology Institute in Life Sciences (ITAV)Centre National de la Recherche Scientifique (CNRS)–USR 3505 Toulouse France

6. Institut de Pharmacologie et de Biologie StructuraleUniversity of Toulouse III–Paul Sabatier Toulouse France

7. Montpellier Cell Biology Research Center (CRBM)CNRS–UMR 5237 Université de Montpellier Montpellier France

8. Centro de Estudos de Doenças Crónicas (CEDOC)Universidade Nova de Lisboa (NOVA) Medical School/Faculdade de Ciências MédicasUniversidade Nova de Lisboa Lisboa Portugal

9. Centre for Clinical ProteomicsOdense University Hospital Odense Denmark

Funder

Institut National Du Cancer

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.201800341RR

Reference37 articles.

1. Mdm2 promotes the rapid degradation of p53

2. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53