Target type: cellularcomponent
A heterodimeric receptor for the cytokine oncostatin-M (OSM). In humans the receptor complex is made up of the gene products gp130 and OSMR-beta. [GOC:jl, PMID:8999038]
The oncostatin-M receptor (OSMR) complex is a transmembrane receptor complex that is activated by the cytokine oncostatin-M (OSM). OSMR is a heterodimer composed of two subunits: the OSM receptor β (OSMRβ) and the gp130 subunit. OSMRβ is the specific receptor for OSM, while gp130 is a shared signaling subunit for several cytokines, including interleukin-6 (IL-6), leukemia inhibitory factor (LIF), and ciliary neurotrophic factor (CNTF).
The OSMR complex is localized to the plasma membrane and is involved in a wide range of cellular processes, including cell proliferation, differentiation, survival, and inflammation. Upon binding of OSM to the OSMRβ subunit, the complex undergoes conformational changes that lead to the recruitment of intracellular signaling molecules. These molecules include the Janus kinase (JAK) family of tyrosine kinases, which phosphorylate the gp130 subunit. Phosphorylated gp130 then recruits signal transducer and activator of transcription (STAT) proteins, which are transcription factors that translocate to the nucleus and regulate gene expression.
The cellular component of the OSMR complex is therefore the plasma membrane. This complex is essential for mediating the biological effects of OSM and plays a critical role in the regulation of diverse cellular functions.'
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Protein | Definition | Taxonomy |
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Interleukin-6 receptor subunit beta | An interleukin-6 receptor subunit beta that is encoded in the genome of human. [PRO:WCB, UniProtKB:P40189] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
madindoline a | madindoline A: inhibits interleukin-6; isolated from Streptomyces; structure in first source | ||
lmt-28 | LMT-28: an interleukin-6 inhibitor that binds gp130; structure in first source |