Cathepsin X cleaves profilin 1 C-Terminal Tyr139 and influences clathrin-mediated endocytosis
Pečar Fonović, Urša (Author), Kos, Janko (Author)

URLURL - Presentation file, Visit http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0137217 This link opens in a new window

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.

Keywords:katepsin X, endocitoza, rak prostate, cisteinski katepsin B, profilin 1, klatrin
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Number of pages:str. 1-14
Numbering:Vol. 10, no. 9
ISSN on article:1932-6203
DOI:10.1371/journal.pone.0137217 Link is opened in a new window
COBISS.SI-ID:3912049 Link is opened in a new window
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Record is a part of a journal

Title:PloS one
Publisher:Public Library of Science
COBISS.SI-ID:2005896 This link opens in a new window

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