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

Hareza, Agnieszka; Bakun, Magda; Świderska, Bianka; Dudkiewicz, Małgorzata; Koscielny, Alicja; Bajur, Anna; Jaworski, Jacek; Dadlez, Michał and Pawłowski, Krzysztof LU (2018) In PeerJ 2018(4).
Abstract

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... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Mass spectrometry, Novel kinases, Phosphoproteomics, Secretory pathway, Signalling
in
PeerJ
volume
2018
issue
4
publisher
PeerJ
external identifiers
  • scopus:85045034931
ISSN
2167-8359
DOI
10.7717/peerj.4599
language
English
LU publication?
yes
id
1fdef120-11bb-4a50-a6e1-4bdc9c1aa8f4
date added to LUP
2018-04-23 13:46:11
date last changed
2019-02-20 11:15:01
@article{1fdef120-11bb-4a50-a6e1-4bdc9c1aa8f4,
  abstract     = {<p>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.</p>},
  articleno    = {4599},
  author       = {Hareza, Agnieszka and Bakun, Magda and Świderska, Bianka and Dudkiewicz, Małgorzata and Koscielny, Alicja and Bajur, Anna and Jaworski, Jacek and Dadlez, Michał and Pawłowski, Krzysztof},
  issn         = {2167-8359},
  keyword      = {Mass spectrometry,Novel kinases,Phosphoproteomics,Secretory pathway,Signalling},
  language     = {eng},
  month        = {01},
  number       = {4},
  publisher    = {PeerJ},
  series       = {PeerJ},
  title        = {Phosphoproteomic insights into processes influenced by the kinase-like protein DIA1/C3orf58},
  url          = {http://dx.doi.org/10.7717/peerj.4599},
  volume       = {2018},
  year         = {2018},
}