ArticleScientific reports2016
Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Structural basis for lipid binding by the blood protein vitronectin, a component of HDL.bioRxiv : the preprint server for biology · 2025Article
- Characterization and regulation of MT1-MMP cell surface-associated activity.Chemical biology & drug design · 2019Article
- MT1-MMP Binds Membranes by Opposite Tips of Its β Propeller to Position It for Pericellular Proteolysis.Structure (London, England : 1993) · 2019Article
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- Tracking the Cartoon mouse phenotype: Hemopexin domain-dependent regulation of MT1-MMP pericellular collagenolytic activity.The Journal of biological chemistry · 2018Article
- Tricine as a convenient scaffold for the synthesis ofTetrahedron letters · 2018Article
- Peripheral membrane associations of matrix metalloproteinases.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017Review
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
Cell surface proteolysis is an integral yet poorly understood physiological process. The present study has examined how the pericellular collagenase membrane-type 1 matrix metalloproteinase (MT1-MMP) and membrane-mimicking environments interplay in substrate binding and processing. NMR derived structural models indicate that MT1-MMP transiently associates with bicelles and cells through distinct residues in blades III and IV of its hemopexin-like domain, while binding of collagen-like triple-helices occurs within blades I and II of this domain. Examination of simultaneous membrane interaction and triple-helix binding revealed a possible regulation of proteolysis due to steric effects of the membrane. At bicelle concentrations of 1%, enzymatic activity towards triple-helices was increased 1.5-fold. A single mutation in the putative membrane interaction region of MT1-MMP (Ser466Pro) resulted in lower enzyme activation by bicelles. An initial structural framework has thus been developed to define the role(s) of cell membranes in modulating proteolysis.
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