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A Unique C‐terminal Domain Allows Retention of Matrix Metalloproteinase‐27 in the Endoplasmic Reticulum
Author(s) -
Cominelli Antoine,
Halbout Mathias,
N'Kuli Francisca,
Lemoine Pascale,
Courtoy Pierre J.,
Marbaix Etienne,
Tyteca Donatienne,
Henriet Patrick
Publication year - 2014
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.12149
Subject(s) - endoplasmic reticulum , er retention , golgi apparatus , matrix metalloproteinase , biology , microbiology and biotechnology , secretory pathway , transmembrane protein , cytosol , subcellular localization , transmembrane domain , cell fractionation , biochemistry , membrane , cytoplasm , enzyme , mutant , receptor , gene
We report that, unlike other matrix metalloproteinases ( MMPs ), MMP ‐27 is retained in the endoplasmic reticulum due to its specific C‐terminal extension ( CTE ). Upon CTE removal, MMP ‐27 accesses the intermediate compartment and Golgi and is constitutively secreted. Conversely, CTE addition to a secreted MMP ( MMP ‐10) causes ER retention and blocks secretion. We further show that MMP ‐27 is not an integral membrane protein. Indeed, the CTE is not a transmembrane domain and MMP ‐27 partitions in the aqueous phase after Triton X‐114 extraction.