O ‐fucosylation of CCN1 is required for its secretion | Zendy

Niwa Yuki | Zendy; Suzuki Takehiro | Zendy; Dohmae Naoshi | Zendy; Simizu Siro | Zendy

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O ‐fucosylation of CCN1 is required for its secretion

Author(s) -

Niwa Yuki,

Suzuki Takehiro,

Dohmae Naoshi,

Simizu Siro

Publication year - 2015

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2015.09.012

Subject(s) - fucosylation , matricellular protein , fucosyltransferase , secretion , thrombospondin , chemistry , microbiology and biotechnology , biochemistry , biology , glycoprotein , enzyme , fucose , extracellular matrix , metalloproteinase

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 Thr 242 . In this report, we demonstrated that CCN1 is O ‐fucosylated at Thr 242 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 Thr 242 regulates its secretion.

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