Structural basis and regulation of the reductive stress response.

Amino Acids / chemistry Animals Carrier Proteins / chemistry Cell Cycle Proteins / chemistry Cell Line Female Humans Ions Mice Mutant Proteins / metabolism Mutation / genetics Protein Binding / drug effects Protein Stability / drug effects Reactive Oxygen Species / metabolism Stress, Physiological / drug effects Structure-Activity Relationship Substrate Specificity / drug effects Ubiquitin-Protein Ligase Complexes / chemistry Ubiquitination / drug effects Zinc / pharmacology
BEX2 BEX3 CUL2 FEM1B mitochondria oxidative phosphorylation reactive oxygen species reductive stress ubiquitin

Journal

Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066

Informations de publication

Date de publication:
14 10 2021
Historique:
received: 22 02 2021
revised: 27 06 2021
accepted: 31 08 2021
pubmed: 26 9 2021
medline: 4 1 2022
entrez: 25 9 2021
Statut: ppublish

Résumé

Although oxidative phosphorylation is best known for producing ATP, it also yields reactive oxygen species (ROS) as invariant byproducts. Depletion of ROS below their physiological levels, a phenomenon known as reductive stress, impedes cellular signaling and has been linked to cancer, diabetes, and cardiomyopathy. Cells alleviate reductive stress by ubiquitylating and degrading the mitochondrial gatekeeper FNIP1, yet it is unknown how the responsible E3 ligase CUL2

Identifiants

DOI: 10.1016/j.cell.2021.09.002 PMID: 34562363 PMC: PMC8810291
pubmed: 34562363
pii: S0092-8674(21)01049-7
doi: 10.1016/j.cell.2021.09.002
pmc: PMC8810291
mid: NIHMS1765725
pii:
doi:

Substances chimiques

Amino Acids 0
Carrier Proteins 0
Cell Cycle Proteins 0
FNIP1 protein, mouse 0
Ions 0
Mutant Proteins 0
Reactive Oxygen Species 0
Fem1b protein, mouse EC 2.3.2.23
Ubiquitin-Protein Ligase Complexes EC 2.3.2.23
Zinc J41CSQ7QDS

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

5375-5390.e16

Subventions

Organisme : NIGMS NIH HHS
ID : T32 GM007232
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM133894
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR025622
Pays : United States
Organisme : NIH HHS
ID : S10 OD021828
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests M.R. and J.K. are co-founders and members of the SAB of Nurix Tx. M.R. is on the SAB of Monte Rosa Tx and an iPartner at The Column Group. J.K. is on the SAB of Revolution Medicine and Carmot Tx.

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Auteurs

Andrew G Manford (AG)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.

Elijah L Mena (EL)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.

Karen Y Shih (KY)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.

Christine L Gee (CL)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.

Rachael McMinimy (R)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

Brenda Martínez-González (B)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

Rumi Sherriff (R)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

Brandon Lew (B)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA.

Madeline Zoltek (M)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

Fernando Rodríguez-Pérez (F)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

Makda Woldesenbet (M)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

John Kuriyan (J)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA 94720, USA; Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Department of Chemistry, University of California at Berkeley, Berkeley, CA 94720, USA.

Michael Rape (M)

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California at Berkeley, Berkeley, CA 94720, USA. Electronic address: mrape@berkeley.edu.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Structural basis and regulation of the...
questionsmedicales.fr › Eucaryotes › Animaux › Structural basis and regulation of the...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Structural basis and regulation of the...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cycle cellulaire › Structural basis and regulation of the...
questionsmedicales.fr › Cellules › Cellules cultivées › Lignée cellulaire › Structural basis and regulation of the...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Structural basis and regulation of the...
questionsmedicales.fr › Produits chimiques inorganiques › Électrolytes › Ions › Structural basis and regulation of the...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Structural basis and regulation of the...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mutantes › Structural basis and regulation of the...
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questionsmedicales.fr › Produits chimiques inorganiques › Composés de l'oxygène › Espèces réactives de l'oxygène › Structural basis and regulation of the...
questionsmedicales.fr › Phénomènes physiologiques › Stress physiologique › Structural basis and regulation of the...
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Relation structure-activité › Structural basis and regulation of the...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › Structural basis and regulation of the...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Structural basis and regulation of the...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › Structural basis and regulation of the...
questionsmedicales.fr › Produits chimiques inorganiques › Métaux › Métaux lourds › Zinc › Structural basis and regulation of the...