| First Author | Morgenstern J | Year | 2020 |
| Journal | Cell Rep | Volume | 32 |
| Issue | 12 | Pages | 108160 |
| PubMed ID | 32966793 | Mgi Jnum | J:306463 |
| Mgi Id | MGI:6715863 | Doi | 10.1016/j.celrep.2020.108160 |
| Citation | Morgenstern J, et al. (2020) Phosphorylation of T107 by CamKIIdelta Regulates the Detoxification Efficiency and Proteomic Integrity of Glyoxalase 1. Cell Rep 32(12):108160 |
| abstractText | 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 Ca(2+)/calmodulin-dependent kinase II delta (CamKIIdelta), 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 CamKIIdelta is associated with poor detoxification capacity and decreased protein content of Glo1 in a murine CamKIIdelta knockout model. Therefore, phosphorylation of T107 in the Glo1 protein by CamKIIdelta is a quick and precise mechanism regulating Glo1 activity, which is experimentally linked to an altered Glo1 status in cancer, diabetes, and during aging. |
