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Membrane type-1 matrix metalloproteinase (MT1-MMP) exhibits an important intracellular cleavage function and causes

Vladislav S Golubkov1, Sarah Boyd, Alexei Y Savinov

  • 1Cancer Research Center, The Burnham Institute, La Jolla, California 92037, USA.

The Journal of Biological Chemistry
|May 10, 2005
PubMed

Insights

Membrane type-1 matrix metalloproteinase (MT1-MMP) has a newly discovered intracellular role. MT1-MMP targets centrosomal proteins, causing chromosome instability and potentially driving cancer development.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • Elevated membrane type-1 matrix metalloproteinase (MT1-MMP) expression is linked to malignancies.
  • Cell surface MT1-MMP is recognized for its role in pericellular proteolysis.

Purpose of the Study:

  • To investigate the intracellular functions of MT1-MMP.
  • To explore the role of MT1-MMP in chromosome instability and malignant transformation.

Main Methods:

  • Tracking MT1-MMP localization within cells.
  • Investigating MT1-MMP interactions with centrosomal proteins.
  • Analyzing mitotic spindle formation and chromosome stability.
  • Examining pericentrin levels in tumor biopsies.

Main Results:

  • MT1-MMP is trafficked along the tubulin cytoskeleton and accumulates in the centrosome.
  • MT1-MMP targets pericentrin, an essential centrosomal protein.
  • MT1-MMP expression induces mitotic aberrations and aneuploidy in non-malignant cells.
  • Tumor biopsies show degraded pericentrin correlating with MT1-MMP activity.

Conclusions:

  • MT1-MMP possesses a novel intracellular function involving pericentrin degradation.
  • This MT1-MMP activity contributes to chromosome instability, a hallmark of early carcinogenesis.
  • The findings elucidate a new proteolytic pathway linking MT1-MMP to malignant transformation.

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