Issue 40, 2019, Issue in Progress
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RSC Advances

Identification of the endoplasmic reticulum localization sequence and N-glycosylation of matrix metalloproteinase 26†

Guangji Zhang,a   Jinrui Zhang,a   Xiang Li,a   Xin Menga  and  Xuexun Fang ORCID logo *a  

* Corresponding authors

a Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, 2699 Qianjin Street, Changchun 130012, PR China
E-mail: fangxx@jlu.edu.cn
Tel: +86-431-85155219

Abstract

Matrix metalloproteinase 26 (MMP-26), also called endometase and matrilysin-2, belongs to the MMP superfamily. Previous studies have focused on its role in tumor invasion and migration but detailed subcellular localization of MMP-26 remains poorly understood. In this study, sequence deletion mutants of MMP-26 revealed that residues 88–123 function to localize MMP-26 to the endoplasmic reticulum (ER). Moreover, using homologous recombination, we show that exchanging residues 88–123 of secretory MMP-7 with the same region in MMP-26 causes localization of this MMP-7 construct to the ER. Moreover, two (N64, N221) of the three possible N-glycosylation sites in MMP-26 were shown to be N-glycosylated, and N-glycosylation is not required for ER localization. These results demonstrate that the 88–123 region of MMP-26 is a noncanonical ER retention signal and MMP-26 is an N-glycosylated protein, thereby providing novel insights into the properties of MMP-26 within the cell.

Graphical abstract: Identification of the endoplasmic reticulum localization sequence and N-glycosylation of matrix metalloproteinase 26

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Article information

DOI
https://doi.org/10.1039/C9RA05222D
Article type
Paper
Submitted
09 Jul 2019
Accepted
20 Jul 2019
First published
25 Jul 2019
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2019,9, 23053-23060

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Identification of the endoplasmic reticulum localization sequence and N-glycosylation of matrix metalloproteinase 26

G. Zhang, J. Zhang, X. Li, X. Meng and X. Fang, RSC Adv., 2019, 9, 23053 DOI: 10.1039/C9RA05222D

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