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Cytokine-Like Factor 1, an Essential Facilitator of Cardiotrophin-Like Cytokine:Ciliary Neurotrophic Factor Receptor α Signaling and sorLA-Mediated Turnover.

Larsen JV, Kristensen AM, Pallesen LT, Bauer J, Vægter CB, Nielsen MS, Madsen P, Petersen CM - Mol. Cell. Biol. (2016)

Bottom Line: The site for CNTFRα enables CLF-1 to promote CLC:CNTFRα complex formation and signaling.The second site establishes a link between the endocytic receptor sorLA and the tripartite CLC:CLF-1:CNTFRα complex and allows sorLA to downregulate the CNTFRα pool in stimulated cells.Finally, sorLA may bind and concentrate the tripartite soluble CLC:CLF-1:CNTFRα complex on cell membranes and thus facilitate its signaling through gp130/LIFRβ.

View Article: PubMed Central - PubMed

Affiliation: The MIND Center, Department of Biomedicine, Aarhus University, Aarhus, Denmark jvl@biomed.au.dk cmp@biomed.au.dk.

No MeSH data available.


Related in: MedlinePlus

SPR analysis: CLF-1-mediated association between sorLA and the CLC-sCNTFRα fusion protein. (A) Binding of CLC-sCNTFRα (100 nM) to immobilized sorLA. (B) As indicated, immobilized sorLA was initially exposed to CLF-1 (100 nM). After binding, the chip was washed in unsupplemented buffer and finally subjected to fresh buffer containing 100 nM CLC-sCNTFRα. The subsequent increase in response units signifies binding of the fusion protein to preformed CLF-1:sorLA complex.
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Figure 2: SPR analysis: CLF-1-mediated association between sorLA and the CLC-sCNTFRα fusion protein. (A) Binding of CLC-sCNTFRα (100 nM) to immobilized sorLA. (B) As indicated, immobilized sorLA was initially exposed to CLF-1 (100 nM). After binding, the chip was washed in unsupplemented buffer and finally subjected to fresh buffer containing 100 nM CLC-sCNTFRα. The subsequent increase in response units signifies binding of the fusion protein to preformed CLF-1:sorLA complex.

Mentions: An additional SPR experiment was set up to determine if the CLC:CLF-1 heterodimer could in fact interact with sorLA and CNTFRα simultaneously. To that end, we first tested binding of a complex of sCNTFRα and CLC, in which the two were connected with a covalent linker peptide to prevent dissociation (CLC:sCNTFRα). As demonstrated by the results shown in Fig. 2A, this construct exhibited no binding activity toward immobilized sorLA, while a significant binding of the construct was seen after pretreatment of sorLA with CLF-1 (Fig. 2B). It can be concluded that CLC:CLF-1 may target both receptors at the same time and thereby constitute a connecting bridge between the two.


Cytokine-Like Factor 1, an Essential Facilitator of Cardiotrophin-Like Cytokine:Ciliary Neurotrophic Factor Receptor α Signaling and sorLA-Mediated Turnover.

Larsen JV, Kristensen AM, Pallesen LT, Bauer J, Vægter CB, Nielsen MS, Madsen P, Petersen CM - Mol. Cell. Biol. (2016)

SPR analysis: CLF-1-mediated association between sorLA and the CLC-sCNTFRα fusion protein. (A) Binding of CLC-sCNTFRα (100 nM) to immobilized sorLA. (B) As indicated, immobilized sorLA was initially exposed to CLF-1 (100 nM). After binding, the chip was washed in unsupplemented buffer and finally subjected to fresh buffer containing 100 nM CLC-sCNTFRα. The subsequent increase in response units signifies binding of the fusion protein to preformed CLF-1:sorLA complex.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4836274&req=5

Figure 2: SPR analysis: CLF-1-mediated association between sorLA and the CLC-sCNTFRα fusion protein. (A) Binding of CLC-sCNTFRα (100 nM) to immobilized sorLA. (B) As indicated, immobilized sorLA was initially exposed to CLF-1 (100 nM). After binding, the chip was washed in unsupplemented buffer and finally subjected to fresh buffer containing 100 nM CLC-sCNTFRα. The subsequent increase in response units signifies binding of the fusion protein to preformed CLF-1:sorLA complex.
Mentions: An additional SPR experiment was set up to determine if the CLC:CLF-1 heterodimer could in fact interact with sorLA and CNTFRα simultaneously. To that end, we first tested binding of a complex of sCNTFRα and CLC, in which the two were connected with a covalent linker peptide to prevent dissociation (CLC:sCNTFRα). As demonstrated by the results shown in Fig. 2A, this construct exhibited no binding activity toward immobilized sorLA, while a significant binding of the construct was seen after pretreatment of sorLA with CLF-1 (Fig. 2B). It can be concluded that CLC:CLF-1 may target both receptors at the same time and thereby constitute a connecting bridge between the two.

Bottom Line: The site for CNTFRα enables CLF-1 to promote CLC:CNTFRα complex formation and signaling.The second site establishes a link between the endocytic receptor sorLA and the tripartite CLC:CLF-1:CNTFRα complex and allows sorLA to downregulate the CNTFRα pool in stimulated cells.Finally, sorLA may bind and concentrate the tripartite soluble CLC:CLF-1:CNTFRα complex on cell membranes and thus facilitate its signaling through gp130/LIFRβ.

View Article: PubMed Central - PubMed

Affiliation: The MIND Center, Department of Biomedicine, Aarhus University, Aarhus, Denmark jvl@biomed.au.dk cmp@biomed.au.dk.

No MeSH data available.


Related in: MedlinePlus