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

Dmitry V. Rozanov, Berhane Ghebrehiwet, Boris I. Ratnikov, Edward Z. Monosov, Elena I. Deryugina, Alex Y. Strongin

Research output: Contribution to journalArticle

45 Scopus citations

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 languageEnglish (US)
Pages (from-to)51-57
Number of pages7
JournalFEBS Letters
Volume527
Issue number1-3
DOIs
StatePublished - Sep 11 2002

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

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