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The Enigma of Tripeptidyl-Peptidase II: Dual Roles in Housekeeping and Stress

By PRETA G., DE KLARK R., GAVIOLI R. and GLAS R.

Abstract

The tripeptidyl-peptidase II complex consists of repeated 138 kDa subunits, assembled into two twisted strands that form a\ud high molecular weight complex (>5MDa). TPPII, like many other cytosolic peptidases, plays a role in the ubiquitin-proteasome\ud pathway downstream of the proteasome as well as in the production and destruction of MHC class I antigens and degradation\ud of neuropeptides. Tripeptidyl-peptidase II activity is increased in cells with an increased demand for protein degradation, but\ud whether degradation of cytosolic peptides is the only cell biological role for TPPII has remained unclear. Recent data indicated that\ud TPPII translocates into the nucleus to control DNA damage responses in malignant cells, supporting that cytosolic “housekeeping\ud peptidases” may have additional roles in cell biology, besides their contribution to protein turnover.Overall, TPPII has an emerging\ud importance in several cancer-related fields, such as metabolism, cell death control, and control of genome integrity; roles that are\ud not understood in detail. The present paper reviews the cell biology of TPPII and discusses distinct roles for TPPII in the nucleus\ud and cytosol

Year: 2010
OAI identifier: oai:iris.unife.it:11392/1561062
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