Critical Reviews™ in Eukaryotic Gene Expression

ISSN for PRINT: 1045-4403

For Online Access

Best Paper Award Selection - Editorial Board Site

2001, Volume11

Issue 4

73 pages

Issue price - $169.00

Loraine Karran
Department of Pathology, Robert Kilpatrick Clinical Sciences Bulding, Leicester Royal Infirmary, Leicester, LE2 7LX, United Kingdom

Martin J. S. Dyer
Department of Pathology, Robert Kilpatrick Clinical Sciences Bulding, Leicester Royal Infirmary, Leicester, LE2 7LX, United Kingdom

Proteolytic modification of certain key regulatory molecules involved in apoptotic and prosurvival pathways may be a feature of the control of programmed cell death. Four molecules of the Bcl-2 family (BID, Bcl-2, Bax, Bcl-X_L) have been reported to be cleaved during apoptosis, as has a cellular inhibitor of apoptosis (XIAP). Two proteins involved in NF-kB activation, RIP and TRAF1, are cleaved during apoptosis induced by agents that activate both pathways. MEKK1, a molecule involved in a protein kinase stress signaling cascade that contributes to apoptosis and NF-kB activation, also undergoes cleavage. In each case, the cleavage products may result in the inactivation of a former function or the gaining of a new function, thus contributing to the delicately balanced regulation of apoptosis.

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