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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.