RRC ID 80944
Author Franziscus CA, Ritz D, Kappel NC, Solinger JA, Schmidt A, Spang A.
Title The protein tyrosine phosphatase PPH-7 is required for fertility and embryonic development in C. elegans at elevated temperatures.
Journal FEBS Open Bio
Abstract Post-translational modifications are key in the regulation of activity, structure, localization, and stability of most proteins in eukaryotes. Phosphorylation is potentially the most studied post-translational modification, also due to its reversibility and thereby the regulatory role this modification often plays. While most research attention was focused on kinases in the past, phosphatases remain understudied, most probably because the addition and presence of the modification is more easily studied than its removal and absence. Here, we report the identification of an uncharacterized protein tyrosine phosphatase PPH-7 in C. elegans, a member of the evolutionary conserved PTPN family of phosphatases. Lack of PPH-7 function led to reduction of fertility and embryonic lethality at elevated temperatures. Proteomics revealed changes in the regulation of targets of the von Hippel-Lindau (VHL) E3 ligase, suggesting a potential role for PPH-7 in the regulation of VHL.
Volume 14(3)
Pages 390-409
Published 2024-3-1
DOI 10.1002/2211-5463.13771
PMID 38320757
PMC PMC10909979
MeSH Animals Caenorhabditis elegans* / metabolism Embryonic Development / genetics Fertility / genetics Protein Tyrosine Phosphatases Temperature Von Hippel-Lindau Tumor Suppressor Protein* / metabolism
C.elegans tm5332 tm5532 tm533