Golgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogen (Q24337919)

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English	Golgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogen	scientific article

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Golgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogen (English)

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Christian Roghi

1

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Louise Jones

2

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Matthew Gratian

3

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William R English

4

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Gillian Murphy

5

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publication date

August 2010

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277

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15

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3158-75

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Membrane type-matrix metalloproteinases (MT-MMP)

1 reference

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MT1-MMP: a potent modifier of pericellular microenvironment.

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The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3.

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Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme

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MT1-MMP: a tethered collagenase

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Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion

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Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets.

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MT1-MMP: universal or particular player in angiogenesis?

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Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP

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Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix.

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Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: importance of MT1-MMP as a therapeutic target for invasive tumors

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Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity

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Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain

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Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity.

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Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis

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The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein

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Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface

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Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal

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Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion

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MT1-MMP expression promotes tumor growth and angiogenesis through an up-regulation of vascular endothelial growth factor expression.

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Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism

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Molecular signature of MT1-MMP: transactivation of the downstream universal gene network in cancer

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Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase

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The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase.

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Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration

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Modulation of the membrane type 1 matrix metalloproteinase cytoplasmic tail enhances tumor cell invasion and proliferation in three-dimensional collagen matrices

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Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors

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Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase

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GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.

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Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55

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Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2

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Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP.

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Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity

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Shedding of membrane type matrix metalloproteinase 5 by a furin-type convertase: a potential mechanism for down-regulation

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cDNA Sequence and mRNA Tissue Distribution of a Novel Human Matrix Metalloproteinase with a Potential Transmembrane Segment

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Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP)

1 reference

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'Shed' furin: mapping of the cleavage determinants and identification of its C-terminus

1 reference

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Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration.

1 reference

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inferred from DOI database lookup

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10.1111/J.1742-4658.2010.07723.X

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30 July 2022

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https://api.fatcat.wiki/v0/release/lio2ndn3nnbkxjmvh6ozvzbmt4

30 July 2022

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https://api.fatcat.wiki/v0/release/lio2ndn3nnbkxjmvh6ozvzbmt4

30 July 2022

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