Phosphoproteomic insights into processes influenced by the kinase-like protein DIA1/C3orf58

Agnieszka Hareza, Magda Bakun, Bianka Świderska, Małgorzata Dudkiewicz, Alicja Koscielny, Anna Bajur, Jacek Jaworski, Michał Dadlez, Krzysztof Pawłowski

Research output: Contribution to journalArticlepeer-review


Many kinases are still 'orphans,' which means knowledge about their substrates, and often also about the processes they regulate, is lacking. Here, DIA1/C3orf58, a member of a novel predicted kinase-like family, is shown to be present in the endoplasmic reticulum and to influence trafficking via the secretory pathway. Subsequently, DIA1 is subjected to phosphoproteomics analysis to cast light on its signalling pathways. A liquid chromatography-tandem mass spectrometry proteomic approach with phosphopeptide enrichment is applied to membrane fractions of DIA1-overexpressing and control HEK293T cells, and phosphosites dependent on the presence of DIA1 are elucidated. Most of these phosphosites belonged to CK2- and proline-directed kinase types. In parallel, the proteomics of proteins immunoprecipitated with DIA1 reported its probable interactors. This pilot study provides the basis for deeper studies of DIA1 signalling.

Original languageEnglish
Article number4599
Issue number4
Publication statusPublished - 2018 Jan 1

Subject classification (UKÄ)

  • Cell and Molecular Biology

Free keywords

  • Mass spectrometry
  • Novel kinases
  • Phosphoproteomics
  • Secretory pathway
  • Signalling


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