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Citation Franziscus CA, Ritz D, Kappel NC, Solinger JA, Schmidt A, Spang A. The protein tyrosine phosphatase PPH-7 is required for fertility and embryonic development in C. elegans at elevated temperatures. FEBS Open Bio, 2024.
PubMed ID 38320757
Short Description The protein tyrosine phosphatase PPH-7 is required for fertility and embryonic development in C. elegans at elevated temperatures.
GEO Record: N.A. Platform: N.A.
Download gene-centric, log2 transformed data: WBPaper00066469.ce.ms.csv
# of Conditions 8
Full Description 1316625150_help 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.
Experimental Details:
MassSpec_WBPaper00066469:N2_rep1
MassSpec_WBPaper00066469:N2_rep2
MassSpec_WBPaper00066469:N2_rep3
MassSpec_WBPaper00066469:pph-7(tm5332)_rep1
MassSpec_WBPaper00066469:pph-7(tm5332)_rep2
MassSpec_WBPaper00066469:pph-7(tm5332)_rep3
MassSpec_WBPaper00066469:pph-7(af5)_rep1
MassSpec_WBPaper00066469:pph-7(af5)_rep2.
Tags 1316625150_help
Method: proteomics, Species: Caenorhabditis elegans, Topic: WT vs. mutant