The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein.
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.
Mesh Terms:
Amino Acid Sequence, Antigens, CD44, Binding Sites, Breast Neoplasms, Carrier Proteins, Cell Compartmentation, Cytoplasm, Humans, Matrix Metalloproteinases, Membrane-Associated, Membrane Glycoproteins, Metalloendopeptidases, Mitochondrial Proteins, Molecular Sequence Data, Peptide Fragments, Precipitin Tests, Receptors, Complement, Tumor Cells, Cultured
Amino Acid Sequence, Antigens, CD44, Binding Sites, Breast Neoplasms, Carrier Proteins, Cell Compartmentation, Cytoplasm, Humans, Matrix Metalloproteinases, Membrane-Associated, Membrane Glycoproteins, Metalloendopeptidases, Mitochondrial Proteins, Molecular Sequence Data, Peptide Fragments, Precipitin Tests, Receptors, Complement, Tumor Cells, Cultured
FEBS Lett.
Date: Sep. 11, 2002
PubMed ID: 12220632
View in: Pubmed Google Scholar
Download Curated Data For This Publication
9722
Switch View:
- Interactions 1