Current Search: ("fieldsg@fau.edu") (x)
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Title
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Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.
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Creator
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Cerofolini, Linda, Amar, Sabrina, Lauer, Janelle L., Martelli, Tommaso, Fragai, Marco, Luchinat, Claudio, Fields, Gregg B.
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Abstract/Description
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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...
Show moreCell 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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Date Issued
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2016-09-13
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PURL
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http://purl.flvc.org/fau/fd/FAUIR0000004
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Format
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Citation
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Title
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The Mechanism by Which MYCN Amplification Confers an Enhanced Sensitivity to a PCNA-Derived Cell Permeable Peptide in Neuroblastoma Cells.
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Creator
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Gu, Long, Chu, Peiguo, Lingeman, Robert, McDaniel, Heather, Kechichian, Steven, Hickey, Robert J., Liu, Zheng, Yuan, Yate-Ching, Sandoval, John A., Fields, Gregg B., Malkas, Linda H.
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Date Issued
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2015-12
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PURL
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http://purl.flvc.org/fau/fd/FAUIR000140
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Format
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Citation
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Title
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Engineered Sarafotoxins as Tissue Inhibitor of Metalloproteinases-like Matrix Metalloproteinase Inhibitors.
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Creator
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Lauer-Fields, Janelle L., Cudic, Mare, Wei, Shuo, Mari, Frank, Fields, Gregg B., Brew, Keith
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Date Issued
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2007-09
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PURL
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http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.1074_jbc.M611612200_1638212835
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Format
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Document (PDF)
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Title
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The Roles of Substrate Thermal Stability and P2 and P1′ Subsite Identity on Matrix Metalloproteinase Triple-helical Peptidase Activity and Collagen Specificity.
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Creator
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Minond, Dmitriy, Lauer-Fields, Janelle L., Cudic, Mare, Overall, Christopher M., Pei, Duanqing, Brew, Keith, Visse, Robert, Nagase, Hideaki, Fields, Gregg B.
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Date Issued
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2006-12
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PURL
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http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.1074_jbc.M606004200_1638203001
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Format
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Document (PDF)
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Title
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Conopeptides and methods of use.
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Creator
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Mari, Frank, Fields, Gregg B., Florida Atlantic University
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Date Issued
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2004-09
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PURL
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http://purl.flvc.org/fcla/dt/15821
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Format
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Document (PDF)
