Biochemical and biophysical research communications
巻
304
号
1
ページ
160 - 166
発行年
2003-04-01
ISSN
0006-291X
DOI
https://doi.org/10.1016/s0006-291x(03)00544-8
出版者
Elsevier
抄録
Membrane-type 1 matrix metalloproteinase (MT1-MMP) is known to be internalized from cell surface, however, the fate of internalized MT1-MMP is still unknown. Here we demonstrate that at least a part of internalized MT1-MMP is targeted for lysosomal proteolysis. Treatment with an inhibitor of lysosomal proteinases chloroquine suppressed degradation of internalized MT1-MMP and induced accumulation of MT1-MMP in CD63-positive lysosomes. Ectopic expression of CD63 accelerated degradation of MT1-MMP, which was blocked by chloroquine. MT1-MMP, and CD63 were shown to form a complex through hemopexin-like domain of MT1-MMP and N-terminal region of CD63, and thus accelerated degradation of MT1-MMP was not observed with mutants lacking these domains. CD63 mutant lacking lysosomal targeting motif was unable to promote MT1-MMP degradation. These results suggest that CD63 regulates MT1-MMP by targeting to lysosomes.
Tetraspanin CD63 Promotes Targetion and Lysosomal Proteolysis of Membrance-Type 1 Matrix Metalloproteinase
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CA-PR-TAKINO-T-Takino[1].BBRC.pdf
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