The modular nature of apoptotic signaling proteins |
| |
Authors: | K Hofmann |
| |
Institution: | MEMOREC Stoffel GmbH, St?ckheimer Weg 1, D-50829 K?ln (Germany), Fax +49 221 950 4848, e-mail: Kay.Hofmann@memorec.com, DE
|
| |
Abstract: | Apoptosis, initiated by a variety of stimuli, is a physiological process that engages a well-ordered signaling cascade, eventually
leading to the controlled death of the cell. The most extensively studied apoptotic stimulus is the binding of death receptors
related to CD95 (Fas/Apo1) by their respective ligands. During the last years, a considerable number of proteins have been
identified which act together in the receptor-proximal part of the signaling pathway. Based on localized regions of sequence
similarity, it has been predicted that these proteins consist of several independently folding domains. In several cases these
predictions have been confirmed by structural studies; in other cases they are at least supported by experimental data. This
review focuses on the three most widespread domain families found in the apoptotic signaling proteins: the death domain, the
death effector domain and the caspase recruitment domain. The recently discovered analogies between these domains, both in
structure and in function, have shed some light on the overall architecture of the pathway leading from death receptor ligation
to the activation of caspases and eventually to the apoptotic phenotype.
Received 8 October 1998; received after revision 8 January 1999; accepted 8 January 1999 |
| |
Keywords: | , Modular, apoptosis, controlled death, structural studies, |
本文献已被 SpringerLink 等数据库收录! |
|