In:
FEBS Letters, Wiley, Vol. 467, No. 2-3 ( 2000-02-11), p. 150-154
Abstract:
We observed fragmentation of an essential proliferation‐related human nuclear protein prothymosin α in the course of apoptosis induced by various stimuli. Prothymosin α cleavage occurred at the DDVD 99 motif. In vitro, prothymosin α could be cleaved at D 99 by caspase‐3 and ‐7. Caspase hydrolysis disrupted the nuclear localization signal of prothymosin α and abrogated the ability of the truncated protein to accumulate inside the nucleus. Prothymosin α fragmentation may therefore be proposed to disable intranuclear proliferation‐related function of prothymosin α in two ways: by cleaving off a short peptide containing important determinants, and by preventing active nuclear uptake of the truncated protein.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(00)01139-X
Language:
English
Publisher:
Wiley
Publication Date:
2000
detail.hit.zdb_id:
1460391-3
SSG:
12