An Atypical Mechanism of SUMOylation of Neurofibromin SecPH Domain Provides New Insights into SUMOylation Site Selection-Reference-Cited by-同舟云学术

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An Atypical Mechanism of SUMOylation of Neurofibromin SecPH Domain Provides New Insights into SUMOylation Site Selection

Published:2024-11 Issue:22 Volume:436 Page:168768
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Bergoug Mohammed,Mosrin Christine,Serrano Amandine,Godin Fabienne,Doudeau Michel,Dundović Iva,Goffinont Stephane,Normand Thierry,Suskiewicz Marcin J.,Vallée Béatrice,Bénédetti Hélène

Funder

CNRS

Ligue Contre le Cancer

Ministère de l'Enseignement supérieur, de la Recherche et de l'Innovation

Agence Nationale de la Recherche

Publisher

Elsevier BV

Reference81 articles.

1. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2;Mahajan;Cell,1997

2. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex;Matunis;J. Cell Biol.,1996

3. Protein modification by SUMO;Johnson;Annu. Rev. Biochem.,2004

4. Function and regulation of SUMO proteases;Hickey;Nature Rev. Mol. Cell Biol.,2012

5. Uncovering SUMOylation dynamics during cell-cycle progression reveals FoxM1 as a key mitotic SUMO target protein;Schimmel;Mol. Cell,2014

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