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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

Overview
Journal FEBS Lett
Specialty Biochemistry
Date 2002 Sep 11
PMID 12220632
Citations 19
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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.

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