Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase 
(MT1-MMP) Structure and Proteolytic Activity.

Cerofolini, Linda; Amar, Sabrina; Lauer, Janelle; Martelli, Tommaso; Fragai, Marco; Luchinat, Claudio; Fields, Gregg B

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.

MPS-Authors

/persons/resource/persons219372

Lauer, Janelle
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Cerofolini, L., Amar, S., Lauer, J., Martelli, T., Fragai, M., Luchinat, C., & Fields, G. B. (2016). Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity. Scientific Reports, 6:.

引用: https://hdl.handle.net/21.11116/0000-0001-028F-C

要旨

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.