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Phosphorylation of T107 by CamKII[delta] regulates the detoxification efficiency and proteomic integrity of glyoxalase 1

The glyoxalase system is a highly conserved and ubiquitously expressed enzyme system, which is responsible for the detoxification of methylglyoxal (MG), a spontaneous by-product of energy metabolism. This study is able to show that a phosphorylation of threonine-107 (T107) in the (rate-limiting) Gly...

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Hauptverfasser: Morgenstern, Jakob (VerfasserIn) , Katz, Sylvia (VerfasserIn) , Krebs-Haupenthal, Jutta (VerfasserIn) , Chen, Jessy (VerfasserIn) , Saadatmand, Ali R. (VerfasserIn) , Garcia Cortizo, Fabiola (VerfasserIn) , Zemva, Johanna (VerfasserIn) , Campos Campos, Marta (VerfasserIn) , Teleman, Aurelio A. (VerfasserIn) , Backs, Johannes (VerfasserIn) , Nawroth, Peter Paul (VerfasserIn) , Fleming, Thomas (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: September 22, 2020
In: Cell reports
Year: 2020, Jahrgang: 32, Heft: 12
ISSN:2211-1247
DOI:10.1016/j.celrep.2020.108160
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.celrep.2020.108160
Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S2211124720311499
Volltext
Verfasserangaben:Jakob Morgenstern, Sylvia Katz, Jutta Krebs-Haupenthal, Jessy Chen, Alireza Saadatmand, Fabiola Garcia Cortizo, Alexandra Moraru, Johanna Zemva, Marta Campos Campos, Aurelio Teleman, Johannes Backs, Peter Nawroth, and Thomas Fleming
Beschreibung
Zusammenfassung:The glyoxalase system is a highly conserved and ubiquitously expressed enzyme system, which is responsible for the detoxification of methylglyoxal (MG), a spontaneous by-product of energy metabolism. This study is able to show that a phosphorylation of threonine-107 (T107) in the (rate-limiting) Glyoxalase 1 (Glo1) protein, mediated by Ca2+/calmodulin-dependent kinase II delta (CamKIIδ), is associated with elevated catalytic efficiency of Glo1 (lower KM; higher Vmax). Additionally, we observe proteasomal degradation of non-phosphorylated Glo1 via ubiquitination does occur more rapidly as compared with native Glo1. The absence of CamKIIδ is associated with poor detoxification capacity and decreased protein content of Glo1 in a murine CamKIIδ knockout model. Therefore, phosphorylation of T107 in the Glo1 protein by CamKIIδ is a quick and precise mechanism regulating Glo1 activity, which is experimentally linked to an altered Glo1 status in cancer, diabetes, and during aging.
Beschreibung:Im Titel wird delta als griechischer Buchstabe dargestellt
Gesehen am 03.11.2020
Beschreibung:Online Resource
ISSN:2211-1247
DOI:10.1016/j.celrep.2020.108160

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