Interacting selectively and non-covalently with TRAIL (TNF-related
apoptosis
inducing ligand), a member of the tumor necrosis factor ligand family that rapidly induces
apoptosis
in a variety of transformed cell lines.
OBSOLETE. Catalysis of the cleavage at the terminal bond of the motif: Asp-Xaa-Xaa-Asp-Xaa. Enzymes with this function are members of the peptidase family C14 and they appear to function in the inactivation of proteins involved in cellular repair and homeostasis during the effector stage of
apoptosis
.
Interacting selectively and non-covalently with the BH1 domain of a protein of the Bcl-2 family. Proteins that act as inhibitors of
apoptosis
harbour at least three BH domains: BH1, BH2 and BH3; the BH1 and BH2 domains are found in all death antagonists of the Bcl-2 family but only in one class of death agonists.
Interacting selectively and non-covalently with the BH2 domain of a protein of the Bcl-2 family. Proteins that act as inhibitors of
apoptosis
harbour at least three BH domains: BH1, BH2 and BH3; the BH1 and BH2 domains are found in all death antagonists of the Bcl-2 family but only in one class of death agonists.
Interacting selectively and non-covalently with a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in
apoptosis-regulatory
proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family.
Interacting selectively and non-covalently with a neurotrophin, any of a family of growth factors that prevent
apoptosis
in neurons and promote nerve growth.
Interacting selectively and non-covalently with a death domain of a protein. The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD bind each other forming oligomers. Some DD-containing proteins are involved in the regulation of
apoptosis
and inflammation through their activation of caspases and NF-kappaB.
Combining with an extracellular messenger (death ligand) without transmission of the signal. Decoy death receptors compete with death receptors for ligand binding, and do not initiate
apoptosis
.
Combining with a neurotrophin, any of a family of growth factors that prevent
apoptosis
in neurons and promote nerve growth, and transmitting the signal to initiate a change in cell activity.
A multisubunit protein complex involved in the signaling phase of the apoptotic process. In mammals it is typically composed of seven Apaf-1 subunits bound to cytochrome c and caspase-9. A similar complex to promote
apoptosis
is formed from homologous gene products in other eukaryotic organisms.
Any dynein complex that catalyzes movement along a cytoplasmic microtubule; cytoplasmic dynein complexes participates in many transport activities in eukaryotes, such as mRNA localization, intermediate filament transport, nuclear envelope breakdown,
apoptosis
, transport of centrosomal proteins, mitotic spindle assembly, virus transport, kinetochore functions, and movement of signaling and spindle checkpoint proteins. Subunits associated with the dynein heavy chain mediate association between dynein heavy chain and cargoes,and may include light chains and light intermediate chains.