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- W2605560387 abstract "Water soluble matrix metalloproteinases (MMPs) have been regarded as diffusing freely in the extracellular matrix. Yet multiple MMPs are also observed at cell surfaces. Their membrane-proximal activities include sheddase activities, collagenolysis, bacterial killing, and intracellular trafficking reaching as far as the nucleus. The catalytic domains of MMP-7 and MMP-12 bind bilayers peripherally, each in two different orientations, by presenting positive charges and a few hydrophobic groups to the surface. Related peripheral membrane associations are predicted for other soluble MMPs. The peripheral membrane associations may support pericellular proteolysis and endocytosis. The isolated soluble domains of MT1-MMP can also associate with membranes. NMR assays suggest transient association of the hemopexin-like domains of MT1-MMP and MMP-12 with lipid bilayers. Peripheral association of soluble MMP domains with bilayers or heparin sulfate proteoglycans probably concentrates them near the membrane. This could increase the probability of forming complexes with membrane-associated proteins, such as those targeted for proteolysis. This article is part of a Special Issue entitled: Matrix Metalloproteinases edited by Rafael Fridman." @default.
- W2605560387 created "2017-04-28" @default.
- W2605560387 creator A5016998490 @default.
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- W2605560387 creator A5053138418 @default.
- W2605560387 creator A5075918296 @default.
- W2605560387 creator A5083326941 @default.
- W2605560387 date "2017-11-01" @default.
- W2605560387 modified "2023-09-25" @default.
- W2605560387 title "Peripheral membrane associations of matrix metalloproteinases" @default.
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