β-cell deletion of the PKm1 and PKm2 isoforms of pyruvate kinase in mice reveals their essential role as nutrient sensors for the K

Adenosine Diphosphate Adenosine Triphosphate / metabolism Amino Acids Animals Mice Nutrients Protein Isoforms Pyruvate Kinase / genetics
ATP/ADP PEP cycle cell biology insulin secretion katp channels mouse pyruvate kinase β-cell metabolism

Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
23 08 2022
Historique:
received: 12 04 2022
accepted: 23 08 2022
pubmed: 24 8 2022
medline: 9 9 2022
entrez: 23 8 2022
Statut: epublish

Résumé

Pyruvate kinase (PK) and the phosphoenolpyruvate (PEP) cycle play key roles in nutrient-stimulated K

Identifiants

DOI: 10.7554/eLife.79422 PMID: 35997256 PMC: PMC9444242
pubmed: 35997256
doi: 10.7554/eLife.79422
pii: 79422
pmc: PMC9444242
doi:
pii:

Substances chimiques

Amino Acids 0
Protein Isoforms 0
Adenosine Diphosphate 61D2G4IYVH
Adenosine Triphosphate 8L70Q75FXE
Pkm protein, mouse EC 2.7.1.40
Pyruvate Kinase EC 2.7.1.40

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIDDK NIH HHS
ID : F31 DK126403
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK113103
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG062328
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK045735
Pays : United States
Organisme : NIDDK NIH HHS
ID : T32 DK007665
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK127637
Pays : United States
Organisme : NIA NIH HHS
ID : T32 AG000213
Pays : United States

Informations de copyright

© 2022, Foster et al.

Déclaration de conflit d'intérêts

HF, TH, EP, SS, SH, SL, HV, SD, RC, MP, RK, MM No competing interests declared

Références

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Auteurs

Hannah R Foster (HR)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Thuong Ho (T)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Evgeniy Potapenko (E)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Sophia M Sdao (SM)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Shih Ming Huang (SM)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Sophie L Lewandowski (SL)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Halena R VanDeusen (HR)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.

Shawn M Davidson (SM)

Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, United States.
Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, United States.

Rebecca L Cardone (RL)

Department of Internal Medicine, Yale University, New Haven, United States.

Marc Prentki (M)

Molecular Nutrition Unit and Montreal Diabetes Research Center, CRCHUM, and Departments of Nutrition, Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Canada.

Richard G Kibbey (RG)

Department of Internal Medicine, Yale University, New Haven, United States.
Department of Cellular & Molecular Physiology, Yale University, New Haven, United States.

Matthew J Merrins (MJ)

Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, University of Wisconsin-Madison, Madison, United States.
William S. Middleton Memorial Veterans Hospital, Madison, United States.
ORCID: 0000-0003-1599-9227

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Classifications MeSH

Recherchemedicale.com › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléotides adényliques › ADP › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléotides adényliques › Adénosine triphosphate › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Acides aminés, peptides et protéines › Acides aminés › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Eucaryotes › Animaux › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Aliments et boissons › Aliments › Nutriments › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Isoformes de protéines › β-cell deletion of the PKm1 and PKm2 isoforms...
Recherchemedicale.com › Enzymes et coenzymes › Enzymes › Transferases › Phosphotransferases › Phosphotransferases (Alcohol Group Acceptor) › Pyruvate kinase › β-cell deletion of the PKm1 and PKm2 isoforms...