Ontology highlight
ABSTRACT:
SUBMITTER: Attali I
PROVIDER: S-EPMC5437815 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
Attali Ilan I Tobelaim William Sam WS Persaud Avinash A Motamedchaboki Khatereh K Simpson-Lavy Kobi J KJ Mashahreh Bayan B Levin-Kravets Olga O Keren-Kaplan Tal T Pilzer Inbar I Kupiec Martin M Wiener Reuven R Wolf Dieter A DA Rotin Daniela D Prag Gali G
The EMBO journal 20170109 4
Ubiquitylation controls protein function and degradation. Therefore, ubiquitin ligases need to be tightly controlled. We discovered an evolutionarily conserved allosteric restraint mechanism for Nedd4 ligases and demonstrated its function with diverse substrates: the yeast soluble proteins Rpn10 and Rvs167, and the human receptor tyrosine kinase FGFR1 and cardiac I<sub>KS</sub> potassium channel. We found that a potential trimerization interface is structurally blocked by the HECT domain α1-heli ...[more]