ArticleThe Journal of biological chemistry2011
Characterization of the dimerization interface of membrane type 4 (MT4)-matrix metalloproteinase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- An epigenome-wide association study of waist circumference in Chinese monozygotic twins.International journal of obesity (2005) · 2024Article
- Molecular Mechanisms Driven by MT4-MMP in Cancer Progression.International journal of molecular sciences · 2023Review
- Matrix Metalloproteinase in Abdominal Aortic Aneurysm and Aortic Dissection.Pharmaceuticals (Basel, Switzerland) · 2019Review
- Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases.International journal of molecular sciences · 2019Review
- MT4-MMP: The GPI-Anchored Membrane-Type Matrix Metalloprotease with Multiple Functions in Diseases.International journal of molecular sciences · 2019Review
- Immunotherapeutic Targeting of Tumor-Associated Blood Vessels.Advances in experimental medicine and biology · 2017Review
- Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities.The Biochemical journal · 2016Review
- Placental membrane-type metalloproteinases (MT-MMPs): Key players in pregnancy.Cell adhesion & migration · 2016Review
- A Disintegrin and Metalloproteinase with Thrombospondin Motifs-5 (ADAMTS-5) Forms Catalytically Active Oligomers.The Journal of biological chemistry · 2016Article
- Drug Development for Metastasis Prevention.Critical reviews in oncogenesis · 2015Review
- Crossing the endothelial barrier during metastasis.Nature reviews. Cancer · 2013Review
- Identification of a high-mannose ICAM-1 glycoform: effects of ICAM-1 hypoglycosylation on monocyte adhesion and outside in signaling.American journal of physiology. Cell physiology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
MT4-MMP (MMP17) belongs to a unique subset of membrane type-matrix metalloproteinases that are anchored to the cell surface via a glycosylphosphatidylinositol moiety. However, little is known about its biochemical properties. Here, we report that MT4-MMP is displayed on the cell surface as a mixed population of monomeric, dimeric, and oligomeric forms. Sucrose gradient fractionation demonstrated that these forms of MT4-MMP are all present in lipid rafts. Mutational and computational analyses revealed that Cys(564), which is present within the stem region, mediates MT4-MMP homodimerization by forming a disulfide bond. Substitution of Cys(564) results in a more rapid MT4-MMP turnover, when compared with the wild-type enzyme, consistent with a role for dimerization in protein stability. Expression of MT4-MMP in Madin-Darby canine kidney cells enhanced cell migration and invasion of Matrigel, a process that requires catalytic activity. However, a serine substitution at Cys(564) did not reduce MT4-MMP-stimulated cell invasion of Matrigel suggesting that homodimerization is not required for this process. Deglycosylation studies showed that MT4-MMP is modified by N-glycosylation. Moreover, inhibition of N-glycosylation by tunicamycin diminished the extent of MT4-MMP dimerization suggesting that N-glycans may confer stability to the dimeric form. Taken together, the data presented here provide a new insight into the characteristics of MT4-MMP and highlight the common and distinct properties of the glycosylphosphatidylinositol-anchored membrane type-matrix metalloproteinases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.