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Functional Roles of N‐Linked Glycosylation of Human Matrix Metalloproteinase 9
Author(s) -
Duellman Tyler,
Burnett John,
Yang Jay
Publication year - 2015
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12312
Subject(s) - endoplasmic reticulum , calreticulin , glycosylation , biology , secretion , glycoprotein , calnexin , n linked glycosylation , er retention , secretory pathway , microbiology and biotechnology , chaperone (clinical) , secretory protein , biochemistry , golgi apparatus , gene , glycan , medicine , pathology , mutant
Matrix metalloproteinase‐9 ( MMP ‐9) is a secreted endoproteinase with two N‐glycosylation sites at residues N38 and N120 . Using bimolecular fluorescence complementation, co‐immunoprecipitation, fluorescence microscopy and extensive site‐directed mutagenesis, we identified the indispensible roles of both N‐glycosylation sites for the secretion of MMP ‐9. The N38 ‐glycosylation‐deficient MMP ‐9 revealed a novel polypeptide‐binding domain that interacted with calreticulin ( CALR ) dependent on the molecular volume of the exposed amino acid. The N120 ‐glycosylation‐deficient MMP ‐9 resulted in reduced secretion stemming from a strong interaction with CALR .