Category: Proteins & Peptides

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Reference: GTX28460

Apoptosis, or programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptosis is induced by certain cytokines including TNF and Fas ligand of the TNFfamily through their death domain (DD) containing receptors, TNFR1 and Fas. The death signals are transduced by a group of DD containing adapter molecules. A novel cell death adapter was recently identified by two independent groups and designated RAIDD (RIP associated ICH1/CED3 homologous protein with DD) and CRADD (caspase and RIP adapter with DD). RAIDD contains a DD and a CARD (for caspase recruitment domain) which interact with RIP and caspase, respectively, to transduce death signals. RAIDD is constitutively expressed in many tissues and mediates apoptosis caused by Fas and TNFR1.

Reference: GTX28461

Apoptosis, or programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptosis is induced by certain cytokines including TNF and Fas ligand of the TNFfamily through their death domain (DD) containing receptors, TNFR1 and Fas. The death signals are transduced by a group of DD containing adapter molecules. A novel cell death adapter was recently identified by two independent groups and designated RAIDD (RIP associated ICH1/CED3 homologous protein with DD) and CRADD (caspase and RIP adapter with DD). RAIDD contains a DD and a CARD (for caspase recruitment domain) which interact with RIP and caspase, respectively, to transduce death signals. RAIDD is constitutively expressed in many tissues and mediates apoptosis caused by Fas and TNFR1.

Reference: GTX28462

This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli. [provided by RefSeq]

Reference: GTX28463

This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli. [provided by RefSeq]

Reference: GTX28464

Certain serine/threonine protein kinases, such as ASK1, RIP, DAP, and ZIP kinases, are mediators of apoptosis. Receptor interacting proteins including RIP and RIP2/RICK mediate apoptosis induced by TNFR1 and Fas, two prototype members in the death receptor family. A novel member in the RIP kinase family was recently identified and designated RIP3. RIP3 contains N-terminal kinase domain but, unlike RIP or RIP2, lacks the C-terminal death or CARD domain. RIP3 binds to RIP and TNFR1, mediates TNFR1 induced apoptosis, and attenuates RIP and TNFR1 induced NF-kB activation. Over expression of RIP3 induces apoptosis and NF-kB activation. The messenger RNA of RIP3 is expressed in a subset of adult tissues.

Reference: GTX29041

Akt (Protein Kinase B, PKB) is a key regulator of many signal transduction pathways (reviewed in ref 1). Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of Akt has been seen in many types of cancer. Akt mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits Akt to the membrane, where it is activated by PDK1 phosphorylation (reviewed in 2). Once phosphorylated, Akt dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. Akt has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation.