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The protein tyrosine phosphatase PPH-7 is required for fertility and embryonic development in C. elegans at elevated temperatures

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.

INSTRUMENT(S): Orbitrap Fusion Lumos, Orbitrap Exploris 480

ORGANISM(S): Caenorhabditis Elegans (ncbitaxon:6239)

SUBMITTER: Alexander Schmidt

PROVIDER: MSV000092663 | MassIVE | Wed Aug 16 01:24:00 BST 2023

SECONDARY ACCESSION(S): PXD044602

REPOSITORIES: MassIVE

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