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  • Cathepsin X cleaves profilin 1 C-Terminal Tyr139 and influences clathrin-mediated endocytosis [Elektronski vir]
    Pečar Fonović, Urša ; Kos, Janko, 1959-
    Cathepsin X, a cysteine carboxypeptidase, is upregulated in several types of cancer. Its molecular target in tumor cells is profilin 1, a known tumor suppressor and regulator of actin cytoskeleton ... dynamics. Cathepsin X cleaves off the C-terminal Tyr139 of profilin 1, affecting binding of poly-L-proline ligands and, consequently, tumor cell migration and invasion. Profilin 1 with mutations at the C-terminus, transiently expressed in prostate cancer cells PC-3, showed that Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis. More profilin 1-clathrin complexes were present in PC-3 cells when cathepsin X was inhibited by its specific inhibitor AMS36 or silenced by siRNA. As a consequence, the endocytosis of FITC-labeled dextran and transferrin conjugate was significantly increased. These results constitute the first report of the regulation of clathrin-mediated endocytosis in tumor cells through proteolytic processing of profilin 1.
    Source: PloS one [Elektronski vir]. - ISSN 1932-6203 (Vol. 10, no. 9, 2015, str. 1-14)
    Type of material - e-article
    Publish date - 2015
    Language - english
    COBISS.SI-ID - 3912049

    Link(s):

    http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0137217
    DOI

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