Dimerization of mitophagy receptor BNIP3L/NIX is essential for recruitment of autophagic machinery.


Journal

Autophagy
ISSN: 1554-8635
Titre abrégé: Autophagy
Pays: United States
ID NLM: 101265188

Informations de publication

Date de publication:
05 2021
Historique:
pubmed: 15 4 2020
medline: 15 12 2021
entrez: 15 4 2020
Statut: ppublish

Résumé

Mitophagy is a conserved intracellular catabolic process responsible for the selective removal of dysfunctional or superfluous mitochondria to maintain mitochondrial quality and need in cells. Here, we examine the mechanisms of receptor-mediated mitophagy activation, with the focus on BNIP3L/NIX mitophagy receptor, proven to be indispensable for selective removal of mitochondria during the terminal differentiation of reticulocytes. The molecular mechanisms of selecting damaged mitochondria from healthy ones are still very obscure. We investigated BNIP3L dimerization as a potentially novel molecular mechanism underlying BNIP3L-dependent mitophagy. Forming stable homodimers, BNIP3L recruits autophagosomes more robustly than its monomeric form. Amino acid substitutions of key transmembrane residues of BNIP3L, BNIP3L

Identifiants

pubmed: 32286918
doi: 10.1080/15548627.2020.1755120
pmc: PMC8143235
doi:

Substances chimiques

Apoptosis Regulatory Proteins 0
BNIP3L protein, human 0
Membrane Proteins 0
Proto-Oncogene Proteins 0
Tumor Suppressor Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1232-1243

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Auteurs

Mija Marinković (M)

School of Medicine, University of Split, Split, Croatia.

Matilda Šprung (M)

Faculty of Science, University of Split, Split, Croatia.

Ivana Novak (I)

School of Medicine, University of Split, Split, Croatia.

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Classifications MeSH