Proteomics

Dataset Information

0

Rufy4 exists as two translationally regulated isoforms, that localize to the mitochondrion in activated macrophages


ABSTRACT: We report here that RUFY4, a newly characterized member of the "RUN and FYVE domain-containing" family of proteins previously associated with autophagy enhancement, is highly expressed in alveolar macrophages (AM). We show that RUFY4 interacts with mitochondria upon stimulation by microbial-associated molecular patterns of AM and dendritic cells. RUFY4 interaction with mitochondria and other organelles is dependent on a previously uncharacterized OmpH domain located immediately upstream of its c-terminal FYVE domain. Further, we demonstrate that Rufy4 mRNA can be translated from an alternative translation initiation codon, giving rise to a N-terminally truncated form of the molecule lacking most of its RUN domain and with enhanced potential for its interaction with mitochondria. Our observations point towards a role of RUFY4 in selective mitochondria clearance in activated phagocytes

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Anshu Bhattacharya  

LAB HEAD: Ivan dikic

PROVIDER: PXD026728 | Pride | 2022-02-17

REPOSITORIES: Pride

altmetric image

Publications

RUFY4 exists as two translationally regulated isoforms, that localize to the mitochondrion in activated macrophages.

Valečka Jan J   Camosseto Voahirana V   McEwan David G DG   Terawaki Seigo S   Liu Zhuangzhuang Z   Strock Eva E   Almeida Catarina R CR   Su Bing B   Dikic Ivan I   Liang Yinming Y   Gatti Evelina E   Pierre Philippe P  

Royal Society open science 20210714 7


We report here that RUFY4, a newly characterized member of the 'RUN and FYVE domain-containing' family of proteins previously associated with autophagy enhancement, is highly expressed in alveolar macrophages (AM). We show that RUFY4 interacts with mitochondria upon stimulation by microbial-associated molecular patterns of AM and dendritic cells. RUFY4 interaction with mitochondria and other organelles is dependent on a previously uncharacterized OmpH domain located immediately upstream of its C  ...[more]

Similar Datasets

2011-04-22 | E-GEOD-28813 | biostudies-arrayexpress
2017-11-08 | E-MTAB-4893 | biostudies-arrayexpress
2017-08-03 | E-MTAB-4720 | biostudies-arrayexpress
2015-03-06 | E-GEOD-59792 | biostudies-arrayexpress
2022-08-09 | PXD030450 | Pride
2015-01-27 | PXD001370 | Pride
2022-05-19 | PXD023790 | Pride
2017-12-15 | GSE107115 | GEO
2024-04-18 | PXD045843 | Pride
2020-06-15 | PXD019042 | Pride