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.
Original language | English (US) |
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Pages (from-to) | 51-57 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 527 |
Issue number | 1-3 |
DOIs | |
State | Published - Sep 11 2002 |
Externally published | Yes |
Keywords
- Extracellular matrix
- Internalization
- Membrane protein
- Membrane type-1 matrix metalloproteinase
- Trafficking
- gC1qR
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology