FEBS Lett. 2002 Sep 11;527(1-3):51-7.

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

Rozanov DV, Ghebrehiwet B, Ratnikov B, Monosov EZ, Deryugina EI, Strongin AY.

Source

The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.

Abstract

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.

PMID:: 12220632; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

LinkOut - more resources

Full Text Sources

Other Literature Sources

COS Scholar Universe

Supplemental Content

Related citations

The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR. [J Biol Chem. 2002]
The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR.
Rozanov DV, Ghebrehiwet B, Postnova TI, Eichinger A, Deryugina EI, Strongin AY. J Biol Chem. 2002 Mar 15; 277(11):9318-25. Epub 2001 Dec 31.
Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells. [Exp Cell Res. 2004]
Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells.
Rozanov DV, Deryugina EI, Monosov EZ, Marchenko ND, Strongin AY. Exp Cell Res. 2004 Feb 1; 293(1):81-95.
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. [J Biol Chem. 2004]
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.
Uekita T, Gotoh I, Kinoshita T, Itoh Y, Sato H, Shiomi T, Okada Y, Seiki M. J Biol Chem. 2004 Mar 26; 279(13):12734-43. Epub 2004 Jan 12.
Review Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion. [Cancer Lett. 2003]
Review Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion.
Seiki M. Cancer Lett. 2003 May 8; 194(1):1-11.
Review Human blood platelet gC1qR/p33. [Immunol Rev. 2001]
Review Human blood platelet gC1qR/p33.
Peerschke EI, Ghebrehiwet B. Immunol Rev. 2001 Apr; 180:56-64.

See reviews... See all...

Cited by 7 PubMed Central articles

A membrane protease regulates energy production in macrophages by activating hypoxia-inducible factor-1 via a non-proteolytic mechanism. [J Biol Chem. 2010]
A membrane protease regulates energy production in macrophages by activating hypoxia-inducible factor-1 via a non-proteolytic mechanism.
Sakamoto T, Seiki M. J Biol Chem. 2010 Sep 24; 285(39):29951-64. Epub 2010 Jul 27.
Peptide aptamers as new tools to modulate clathrin-mediated internalisation--inhibition of MT1-MMP internalisation. [BMC Cell Biol. 2010]
Peptide aptamers as new tools to modulate clathrin-mediated internalisation--inhibition of MT1-MMP internalisation.
Wickramasinghe RD, Ko Ferrigno P, Roghi C. BMC Cell Biol. 2010 Jul 23; 11:58. Epub 2010 Jul 23.
Mitochondrial p32 protein is a critical regulator of tumor metabolism via maintenance of oxidative phosphorylation. [Mol Cell Biol. 2010]
Mitochondrial p32 protein is a critical regulator of tumor metabolism via maintenance of oxidative phosphorylation.
Fogal V, Richardson AD, Karmali PP, Scheffler IE, Smith JW, Ruoslahti E. Mol Cell Biol. 2010 Mar; 30(6):1303-18. Epub 2010 Jan 25.

See all...

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Gene
Gene records that cite the current articles. Citations in Gene are added manually by NCBI or imported from outside public resources.
Gene (GeneRIF)
Gene records that have the current articles as Reference into Function citations (GeneRIFs). NLM staff reviewing the literature while indexing MEDLINE add GeneRIFs manually.
HomoloGene
HomoloGene clusters of homologous genes and sequences that cite the current articles. These are references on the Gene and sequence records in the HomoloGene entry.
Nucleotide (RefSeq)
NCBI nucleotide Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.
Nucleotide (Weighted)
Nucleotide records associated with the current articles through the Gene database. These are the related sequences on the Gene record that are added manually by NCBI.
Protein (RefSeq)
NCBI protein Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.
Protein (Weighted)
Protein records associated with the current articles through related Gene database records. These are the related sequences on the Gene record that are added manually by NCBI.
Taxonomy via GenBank
Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
UniGene
UniGene clusters of expressed sequences that are associated with the current articles through references on the clustered sequence records and related Gene records.
GEO Profiles
Gene Expression Omnibus (GEO) Profiles of molecular abundance data. The current articles are references on the Gene record associated with the GEO profile.
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinas...
The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein.
FEBS Lett. 2002 Sep 11 ;527(1-3):51-7.

PubMed
Liver metastasis in a case of adenoid cystic carcinoma of the Bartholin's gland:...
Liver metastasis in a case of adenoid cystic carcinoma of the Bartholin's gland: a rare presentation.
Arch Gynecol Obstet. 2009 May ;279(5):747-50. Epub 2008 Sep 18 .

PubMed
Activation of cryptic 3' splice sites within introns of cellular genes following...
Activation of cryptic 3' splice sites within introns of cellular genes following gene entrapment.
Nucleic Acids Res. 2004 May 20 ;32(9):2912-24. Print 2004 .

PubMed
Activity of pyruvate dehydrogenase A (PDHA) in hamster spermatozoa correlates po...
Activity of pyruvate dehydrogenase A (PDHA) in hamster spermatozoa correlates positively with hyperactivation and is associated with sperm capacitation.
Biol Reprod. 2006 Nov ;75(5):767-77. Epub 2006 Jul 19 .

PubMed
Assessing public health capabilities during emergency preparedness tabletop exer...
Assessing public health capabilities during emergency preparedness tabletop exercises: reliability and validity of a measurement tool.
Public Health Rep. 2009 Jan-Feb ;124(1):138-48.

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Display Settings:

Send to:

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

Source

Abstract

Publication Types, MeSH Terms, Substances, Grant Support

Publication Types

MeSH Terms

Substances

Grant Support

LinkOut - more resources

Full Text Sources

Other Literature Sources

Supplemental Content

Related citations

Cited by 7 PubMed Central articles

Related information

Recent activity

Simple NCBI Directory

Getting Started

Resources

Popular

Featured

NCBI Information