Cancer and Metastasis Reviews

, Volume 25, Issue 1, pp 87–98

Mislocalization and unconventional functions of cellular MMPs in cancer


DOI: 10.1007/s10555-006-7892-y

Cite this article as:
Strongin, A.Y. Cancer Metastasis Rev (2006) 25: 87. doi:10.1007/s10555-006-7892-y


MMPs are multifunctional enzymes capable of targeting the extracellular matrix, growth factors, cytokines and cell surface-associated adhesion and signaling receptors. The cellular localization and the activity of MMPs are tightly controlled at both the transcriptional and the post-transcriptional levels. Mislocalization and presentation in unconventional cellular compartments provide MMPs with an opportunity to cleave previously unidentified proteins. This review is focused on two, entirely different MMPs, one of which is membrane-tethered and another of which is soluble (MT1-MMP and MMP-26, respectively) from twenty four known human MMPs. Our recent studies determined that both of these enzymes functioned at unexpected cellular compartments and it was resulted in the identification of novel proteolytic pathways, whose significance we only partially comprehend as of this writing. It is reasonable, however, to hypothesize from these data that many individual MMPs perform in a similar manner and display a much broader range of functions compared to what we earlier thought.


MMPs, MMP-26, MT1-MMP Migration Invasion Tumorigenesis Pericentrin Centrosome Aneuploidy 



cytoplasmic tail


ductal carcinoma in situ

ERα anf ERβ

estrogen receptor-α and -β, respectively


extracellular matrix


estrogen response element


green fluorescent protein


matrix metalloproteinase

MT1-, MT2-, MT3-, MT4-, MT5- and MT6-MMP

membrane type-1, -2, -3, -4, -5 and -6 matrix metalloproteinase, respectively


small interfering RNA


tissue inhibitor of matrix metalloproteinases


vascular endothelial growth factor

Copyright information

© Springer Science + Business Media, LLC 2006

Authors and Affiliations

  1. 1.The Burnham Institute for Medical ResearchLa Jolla