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Signal transduction subunit

Modrell, B., Liu, J., Miller, H. and Shoyab, M. (1994) LIF and OM directly interact with a soluble form of gpl30, the IL-6 receptor signal transduction subunit. Growth Factors 11 81-91. [Pg.287]

Chaperones. Figure 2 The multiple roles of BiP in the biogenesis of the secretory proteins. BiP, immunoglobulin heavy chain binding protein ER, endoplasmic reticulum ERAD, ER-associated degradation ERj, resident ER protein with J-domain Sec61, core subunit of the protein translocase UPR, unfolded protein response that involves several signal transduction pathways that are activated in order to increase the biosynthetic capacity and decrease the biosynthetic burden of the ER... [Pg.350]

G protein p-3 subunit Truncated protein with increased signal transduction in carriers of the 825T allele. Associated with hypertension and with the response to thiazide diuretics. [Pg.950]

Histidine phosphatases and aspartate phosphatases are well established in lower organisms, mainly in bacteria and in context with two-component-systems . Reversible phosphorylation of histidine residues in vertebrates is in its infancy. The first protein histidine phosphatase (PHP) from mammalian origin was identified just recently. The soluble 14 kD protein does not resemble any of the other phosphatases. ATP-citrate lyase and the (3-subunit of heterotrimeric GTP-binding proteins are substrates of PHP thus touching both, metabolic pathways and signal transduction [4]. [Pg.1014]

Figure 8.1 Cytokine receptors usually display a unique cytokine ( ligand )-binding domain, but they share additional receptor components that are normally responsible for signal transduction. This explains the molecular basis of pleiotropy. IL-6, IL-11 and LIF receptors, for example, are all composed of a distinct ligand-specific binding domain and a separate subunit (gp 130). gp 130 is responsible for initiating signal transduction and is identical in all three receptors. This is depicted schematically above... Figure 8.1 Cytokine receptors usually display a unique cytokine ( ligand )-binding domain, but they share additional receptor components that are normally responsible for signal transduction. This explains the molecular basis of pleiotropy. IL-6, IL-11 and LIF receptors, for example, are all composed of a distinct ligand-specific binding domain and a separate subunit (gp 130). gp 130 is responsible for initiating signal transduction and is identical in all three receptors. This is depicted schematically above...
The oligosaccharide components play a direct and central role in the biosynthesis, secretion, serum half-life and potency of the gonadotrophins. The sugar components attached to the a-subu-nits play an important role in dimer assembly and stability, as well as hormone secretion and possibly signal transduction. The sugars associated with the P-subunit, while contributing to dimer assembly and secretion, appear to play a more prominent role in clearance of the hormone from circulation. [Pg.313]

GM-CSF and IL-3 have been shown to compete for receptors in some types of cells (e.g. eosinophils and KG-1 cells), indicating some structural homology between GM-CSF and IL-3 receptors, perhaps because they share certain subunits or adapter proteins. GM-CSF occupancy results in phosphorylation of certain proteins, and because the receptor possesses no inherent kinase activity, receptor occupancy must be linked to kinase activity via the generation of second messenger molecules. Pretreatment of cells with pertussis toxin abolishes the effects of GM-CSF, indicating the involvement of G-proteins in signal transduction. Priming of neutrophil functions with GM-CSF involves the activation of phospholipases A2 and D. [Pg.47]


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See also in sourсe #XX -- [ Pg.260 , Pg.261 ]




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