FBP2-A New Player in Regulation of Motility of Mitochondria and Stability of Microtubules in Cardiomyocytes.


Journal

Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052

Informations de publication

Date de publication:
21 05 2022
Historique:
received: 21 04 2022
revised: 18 05 2022
accepted: 19 05 2022
entrez: 28 5 2022
pubmed: 29 5 2022
medline: 1 6 2022
Statut: epublish

Résumé

Recently, we have shown that the physiological roles of a multifunctional protein fructose 1,6-bisphosphatase 2 (FBP2, also called muscle FBP) depend on the oligomeric state of the protein. Here, we present several lines of evidence that in HL-1 cardiomyocytes, a forced, chemically induced reduction in the FBP2 dimer-tetramer ratio that imitates AMP and NAD

Identifiants

pubmed: 35626746
pii: cells11101710
doi: 10.3390/cells11101710
pmc: PMC9139521
pii:
doi:

Substances chimiques

Tubulin 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

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Auteurs

Łukasz Pietras (Ł)

Department of Molecular Physiology and Neurobiology, University of Wrocław, Sienkiewicza 21, 50-335 Wrocław, Poland.

Ewa Stefanik (E)

Department of Molecular Physiology and Neurobiology, University of Wrocław, Sienkiewicza 21, 50-335 Wrocław, Poland.

Dariusz Rakus (D)

Department of Molecular Physiology and Neurobiology, University of Wrocław, Sienkiewicza 21, 50-335 Wrocław, Poland.

Agnieszka Gizak (A)

Department of Molecular Physiology and Neurobiology, University of Wrocław, Sienkiewicza 21, 50-335 Wrocław, Poland.

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Classifications MeSH