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