PMID- 10442092
OWN - NLM
STAT- MEDLINE
DCOM- 19990907
LR  - 20191103
IS  - 1420-682X (Print)
IS  - 1420-682X (Linking)
VI  - 55
IP  - 8-9
DP  - 1999 Jul
TI  - The modular nature of apoptotic signaling proteins.
PG  - 1113-28
AB  - 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.
FAU - Hofmann, K
AU  - Hofmann K
AD  - MEMOREC Stoffel GmbH, Koln, Germany. Kay.Hofmann@memorec.com
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Switzerland
TA  - Cell Mol Life Sci
JT  - Cellular and molecular life sciences : CMLS
JID - 9705402
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Antigens, CD)
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (FADD protein, human)
RN  - 0 (FASLG protein, human)
RN  - 0 (Fas Ligand Protein)
RN  - 0 (Fas-Associated Death Domain Protein)
RN  - 0 (Helminth Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Tumor Necrosis Factor)
RN  - 0 (Receptors, Tumor Necrosis Factor, Type I)
RN  - 0 (TNF Receptor-Associated Factor 1)
RN  - 0 (fas Receptor)
RN  - EC 1.14.19.- (Fatty Acid Desaturases)
RN  - EC 1.14.99.- (Fad7 protein, Arabidopsis)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (RIPK1 protein, human)
RN  - EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases)
RN  - EC 3.4.22.- (Caspases)
SB  - IM
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Antigens, CD/chemistry/physiology
MH  - *Apoptosis
MH  - *Arabidopsis Proteins
MH  - Carrier Proteins/chemistry/physiology
MH  - Caspases/metabolism
MH  - Enzyme Activation
MH  - Fas Ligand Protein
MH  - Fas-Associated Death Domain Protein
MH  - Fatty Acid Desaturases/chemistry/physiology
MH  - Helminth Proteins/chemistry/physiology
MH  - Humans
MH  - Infant, Newborn
MH  - Membrane Glycoproteins/chemistry/physiology
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - *Protein Structure, Tertiary
MH  - Protein-Serine-Threonine Kinases/chemistry/physiology
MH  - Proteins/chemistry/physiology
MH  - Receptor-Interacting Protein Serine-Threonine Kinases
MH  - Receptors, Tumor Necrosis Factor/chemistry/physiology
MH  - Receptors, Tumor Necrosis Factor, Type I
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - *Signal Transduction
MH  - Structure-Activity Relationship
MH  - TNF Receptor-Associated Factor 1
MH  - fas Receptor/chemistry/physiology
RF  - 108
EDAT- 1999/08/12 00:00
MHDA- 1999/08/12 00:01
CRDT- 1999/08/12 00:00
PHST- 1999/08/12 00:00 [pubmed]
PHST- 1999/08/12 00:01 [medline]
PHST- 1999/08/12 00:00 [entrez]
AID - 10.1007/s000180050361 [doi]
PST - ppublish
SO  - Cell Mol Life Sci. 1999 Jul;55(8-9):1113-28. doi: 10.1007/s000180050361.