Ontology highlight
ABSTRACT:
SUBMITTER: Stangl A
PROVIDER: S-EPMC6754446 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Stangl Aurelia A Elliott Paul R PR Pinto-Fernandez Adan A Bonham Sarah S Harrison Luke L Schaub Annalisa A Kutzner Kerstin K Keusekotten Kirstin K Pfluger Paul T PT El Oualid Farid F Kessler Benedikt M BM Komander David D Krappmann Daniel D
Nature communications 20190920 1
OTULIN (OTU Deubiquitinase With Linear Linkage Specificity) specifically hydrolyzes methionine1 (Met1)-linked ubiquitin chains conjugated by LUBAC (linear ubiquitin chain assembly complex). Here we report on the mass spectrometric identification of the OTULIN interactor SNX27 (sorting nexin 27), an adaptor of the endosomal retromer complex responsible for protein recycling to the cell surface. The C-terminal PDZ-binding motif (PDZbm) in OTULIN associates with the cargo-binding site in the PDZ do ...[more]