Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Intracellular Signaling Affects Focal Adhesions

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

Translocation of Proteins into the Mitochondria

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,...

Overview of Cell-Matrix Interactions

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...

Cell-matrix's Response to Mechanical Forces

Cell-matrix's Response to Mechanical Forces

In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue.
Anchoring junctions mechanically attach a cell to the...

Cytoskeletal Coordination in Cell Migration

Cytoskeletal Coordination in Cell Migration

A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...

Microtubule Associated Proteins (MAPs)

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

[Diagnosis and treatment of acute pulmonary embolism].

Radiologie (Heidelberg, Germany)·2025

Same author

[Diagnosis and treatment of acute pulmonary embolism].

Medizinische Klinik, Intensivmedizin und Notfallmedizin·2025

Same author

Target organ toxicity in Sprague Dawley rats following oral exposure to complex groundwater mixture: Assessment of dose-response relationships using histopathological and biochemical alterations.

Regulatory toxicology and pharmacology : RTP·2024

Same author

Impaired memory in Sprague-Dawley rats exposed to complex groundwater mixtures of contaminants is associated with reduced cranial blood flow and hippocampal neurotoxicity.

Neurotoxicology·2024

Same author

Linking pesticide exposure to neurodegenerative diseases: An in vitro investigation with human neuroblastoma cells.

The Science of the total environment·2024

Same author

Herbicides and pesticides synergistically interact at low concentrations in complex mixtures.

Chemosphere·2024

Search research articles

Related Experiment Video

Updated: May 13, 2026

Single-Molecule Localization Microscopy of Membrane Proteins using Single-Antibody Labeling

Single-Molecule Localization Microscopy of Membrane Proteins using Single-Antibody Labeling

Published on: March 20, 2026

The tetraspanin network modulates MT1-MMP cell surface trafficking.

H M Schröder¹, S C Hoffmann, M Hecker

¹Institute of Physiology and Pathophysiology, Division of Cardiovascular Physiology, Heidelberg University, 69120 Heidelberg, Germany. h.schroeder@physiologie.uni-heidelberg.de

The International Journal of Biochemistry & Cell Biology

|March 19, 2013

Summary

Tetraspanins regulate the cell surface expression and function of membrane-type 1 matrix metalloproteinase (MT1-MMP). These interactions, occurring in the endoplasmic reticulum, control MT1-MMP

More Related Videos

Nanopodia - Thin, Fragile Membrane Projections with Roles in Cell Movement and Intercellular Interactions

Nanopodia - Thin, Fragile Membrane Projections with Roles in Cell Movement and Intercellular Interactions

Published on: April 3, 2014

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Related Experiment Videos

Last Updated: May 13, 2026

Single-Molecule Localization Microscopy of Membrane Proteins using Single-Antibody Labeling

Single-Molecule Localization Microscopy of Membrane Proteins using Single-Antibody Labeling

Published on: March 20, 2026

Nanopodia - Thin, Fragile Membrane Projections with Roles in Cell Movement and Intercellular Interactions

Nanopodia - Thin, Fragile Membrane Projections with Roles in Cell Movement and Intercellular Interactions

Published on: April 3, 2014

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Membrane-type 1 matrix metalloproteinase (MT1-MMP) is crucial for physiological and pathophysiological processes, including extracellular matrix degradation and MMP-2 activation.
Cell surface expression and trafficking of MT1-MMP are key regulators of its proteolytic activity.
Tetraspanins are membrane proteins known to organize membrane microdomains and regulate the trafficking of associated proteins.

Purpose of the Study:

To investigate the interaction between MT1-MMP and tetraspanins.
To determine the effects of tetraspanin association on MT1-MMP intracellular trafficking.
To elucidate the impact of tetraspanin binding on MT1-MMP proteolytic function.

Main Methods:

Yeast two-hybrid screening to identify interacting proteins.
Immunoprecipitation to confirm MT1-MMP interactions with tetraspanins and MAL.
Analysis of MT1-MMP truncation constructs and mutants to map interaction domains.
Subcellular localization studies using models of post-translational processing.
Functional assays measuring pro-MMP-2 activation and collagen invasion.

Main Results:

MT1-MMP interacts with EWI-2, and stably associates with tetraspanins (CD9, CD37, CD53, CD63, CD81, CD82) and MAL.
The hemopexin domain of MT1-MMP mediates interaction with tetraspanins and MAL.
Interactions occur in the endoplasmic reticulum and are independent of MT1-MMP O-glycosylation.
Tetraspanins differentially modulate MT1-MMP cell surface localization, pro-MMP-2 activation, and collagen invasion capacity.
The extent of tetraspanin-MT1-MMP association did not correlate with functional impact.

Conclusions:

Tetraspanins and MAL bind to the hemopexin domain of MT1-MMP during its endoplasmic reticulum processing.
Tetraspanins distinctly regulate MT1-MMP subcellular localization and proteolytic functions.
Tetraspanin networks offer a mechanism to control MT1-MMP activity at the cell surface.