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Updated: Oct 27, 2025

Functional Characterization of Endogenously Expressed Human RYR1 Variants
Published on: June 9, 2021
RUFY4 exists as two translationally regulated isoforms, that localize to the mitochondrion in activated macrophages
Jan Valečka1, Voahirana Camosseto1, David G McEwan2
1Aix Marseille Université, CNRS, INSERM, CIML, 13288 Marseille cedex 9, France.
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 messenger RNA 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.
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