rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2002-9-10
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pubmed:abstractText |
Membrane type-1 matrix metalloproteinase (MT1-MMP), a key enzyme in cell locomotion, is known to be primarily recruited to the leading edge of migrating cells. This raises a possibility that the C-terminal cytoplasmic tail of MT1-MMP interacts with intracellular regulatory proteins, which modulate translocations of the protease across the cell. Here, we demonstrated that MT1-MMP via its cytoplasmic tail directly associates with a chaperone-like compartment-specific regulator gC1qR. Although a direct functional link between these two proteins remains uncertain, our observations suggest that the transient associations of gC1qR with the cytoplasmic tail of MT1-MMP are likely to be involved in the mechanisms regulating presentation of the protease at the tumor cell surface.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/C1QBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/complement 1q receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
527
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12220632-Amino Acid Sequence,
pubmed-meshheading:12220632-Antigens, CD44,
pubmed-meshheading:12220632-Binding Sites,
pubmed-meshheading:12220632-Breast Neoplasms,
pubmed-meshheading:12220632-Carrier Proteins,
pubmed-meshheading:12220632-Cell Compartmentation,
pubmed-meshheading:12220632-Cytoplasm,
pubmed-meshheading:12220632-Humans,
pubmed-meshheading:12220632-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:12220632-Membrane Glycoproteins,
pubmed-meshheading:12220632-Metalloendopeptidases,
pubmed-meshheading:12220632-Mitochondrial Proteins,
pubmed-meshheading:12220632-Molecular Sequence Data,
pubmed-meshheading:12220632-Peptide Fragments,
pubmed-meshheading:12220632-Precipitin Tests,
pubmed-meshheading:12220632-Receptors, Complement,
pubmed-meshheading:12220632-Tumor Cells, Cultured
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pubmed:year |
2002
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pubmed:articleTitle |
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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pubmed:affiliation |
The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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