Related Experiment Video

Updated: Sep 24, 2025

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

2.3K

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

Guangji Zhang1, Jinrui Zhang1, Xiang Li1

  • 1Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University 2699 Qianjin Street Changchun 130012 PR China fangxx@jlu.edu.cn +86-431-85155219.

RSC Advances
|May 6, 2022
PubMed

Insights

Matrix metalloproteinase 26 (MMP-26) is localized to the endoplasmic reticulum (ER) via residues 88-123. This region acts as a noncanonical ER retention signal, offering new insights into MMP-26 cellular properties.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Matrix metalloproteinase 26 (MMP-26), also known as endometase or matrilysin-2, is part of the MMP superfamily.
  • While MMP-26's role in tumor invasion and migration is studied, its precise subcellular localization is not well understood.

Purpose of the Study:

  • To determine the subcellular localization of MMP-26.
  • To identify the specific regions responsible for MMP-26 localization.
  • To investigate the role of N-glycosylation in MMP-26 localization.

Main Methods:

  • Sequence deletion mutants of MMP-26 were created to identify localization signals.
  • Homologous recombination was used to swap regions between MMP-26 and MMP-7.
  • N-glycosylation sites were analyzed to assess their impact on localization.

Main Results:

  • Residues 88-123 of MMP-26 were identified as crucial for its localization to the endoplasmic reticulum (ER).
  • Transferring the 88-123 region from MMP-26 to MMP-7 directed the MMP-7 construct to the ER.
  • Two of three potential N-glycosylation sites (N64, N221) were found to be N-glycosylated, but this modification was not essential for ER localization.

Conclusions:

  • The 88-123 region of MMP-26 functions as a noncanonical ER retention signal.
  • MMP-26 is an N-glycosylated protein.
  • These findings provide novel insights into the intracellular properties and localization of MMP-26.

More Related Videos

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells10:24

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

14.4K
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.7K

Related Concept Videos

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.1K
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.7K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
5.0K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.9K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
9.2K