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 Letters

Volumn 527, Issue 1-3, 2002, Pages 51-57

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

^a BURNHAM INSTITUTE   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

Extracellular matrix; gC1qR; Internalization; Membrane protein; Membrane type 1 matrix metalloproteinase; Trafficking

Indexed keywords

CHAPERONE; MATRIX METALLOPROTEINASE 14; PROTEINASE; REGULATOR PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MIGRATION; CELL SURFACE; CONTROLLED STUDY; CYTOPLASM; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN INTERACTION; TUMOR CELL;

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;

EID: 0037063349     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(02)03153-8     Document Type: Article

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