O-fucosylation of CCN1 is required for its secretion

Yuki Niwa, Takehiro Suzuki, Naoshi Dohmae, Siro Simizu

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)


The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions. Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr242. In this report, we demonstrated that CCN1 is O-fucosylated at Thr242 using mass spectrometry. Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1. Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1. These results demonstrated that O-fucosylation of CCN1 at Thr242 regulates its secretion.

Original languageEnglish
Pages (from-to)3287-3293
Number of pages7
JournalFEBS Letters
Issue number21
Publication statusPublished - 2015 Oct 24


  • CCN1
  • Glycosylation
  • Mass spectrometry
  • O-fucosylation
  • Protein O-fucosyltransferase2 (Pofut2)

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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