The molecular basis of chaperone-mediated interleukin 23 assembly control
It is unclear how unassembled secretory pathway proteins are discriminated from misfolded ones. Here the authors combine biophysical and cellular experiments to study the folding of heterodimeric interleukin 23 and describe how ER chaperones recognize unassembled proteins and aid their assembly into...
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Nature Portfolio
2019
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oai:doaj.org-article:7a8999f450d04116918a03d1d6abd2582021-12-02T14:35:44ZThe molecular basis of chaperone-mediated interleukin 23 assembly control10.1038/s41467-019-12006-x2041-1723https://doaj.org/article/7a8999f450d04116918a03d1d6abd2582019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12006-xhttps://doaj.org/toc/2041-1723It is unclear how unassembled secretory pathway proteins are discriminated from misfolded ones. Here the authors combine biophysical and cellular experiments to study the folding of heterodimeric interleukin 23 and describe how ER chaperones recognize unassembled proteins and aid their assembly into protein complexes while preventing the premature degradation of unassembled units.Susanne MeierSina BohnackerCarolin J. KloseAbraham LopezChristian A. ChoePhilipp W. N. SchmidNicolas BloemekeFlorian RührnößlMartin HaslbeckJulia Esser-von BierenMichael SattlerPo-Ssu HuangMatthias J. FeigeNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Susanne Meier Sina Bohnacker Carolin J. Klose Abraham Lopez Christian A. Choe Philipp W. N. Schmid Nicolas Bloemeke Florian Rührnößl Martin Haslbeck Julia Esser-von Bieren Michael Sattler Po-Ssu Huang Matthias J. Feige The molecular basis of chaperone-mediated interleukin 23 assembly control |
| description |
It is unclear how unassembled secretory pathway proteins are discriminated from misfolded ones. Here the authors combine biophysical and cellular experiments to study the folding of heterodimeric interleukin 23 and describe how ER chaperones recognize unassembled proteins and aid their assembly into protein complexes while preventing the premature degradation of unassembled units. |
| format |
article |
| author |
Susanne Meier Sina Bohnacker Carolin J. Klose Abraham Lopez Christian A. Choe Philipp W. N. Schmid Nicolas Bloemeke Florian Rührnößl Martin Haslbeck Julia Esser-von Bieren Michael Sattler Po-Ssu Huang Matthias J. Feige |
| author_facet |
Susanne Meier Sina Bohnacker Carolin J. Klose Abraham Lopez Christian A. Choe Philipp W. N. Schmid Nicolas Bloemeke Florian Rührnößl Martin Haslbeck Julia Esser-von Bieren Michael Sattler Po-Ssu Huang Matthias J. Feige |
| author_sort |
Susanne Meier |
| title |
The molecular basis of chaperone-mediated interleukin 23 assembly control |
| title_short |
The molecular basis of chaperone-mediated interleukin 23 assembly control |
| title_full |
The molecular basis of chaperone-mediated interleukin 23 assembly control |
| title_fullStr |
The molecular basis of chaperone-mediated interleukin 23 assembly control |
| title_full_unstemmed |
The molecular basis of chaperone-mediated interleukin 23 assembly control |
| title_sort |
molecular basis of chaperone-mediated interleukin 23 assembly control |
| publisher |
Nature Portfolio |
| publishDate |
2019 |
| url |
https://doaj.org/article/7a8999f450d04116918a03d1d6abd258 |
| work_keys_str_mv |
AT susannemeier themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT sinabohnacker themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT carolinjklose themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT abrahamlopez themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT christianachoe themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT philippwnschmid themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT nicolasbloemeke themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT florianruhrnoßl themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT martinhaslbeck themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT juliaesservonbieren themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT michaelsattler themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT possuhuang themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT matthiasjfeige themolecularbasisofchaperonemediatedinterleukin23assemblycontrol AT susannemeier molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT sinabohnacker molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT carolinjklose molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT abrahamlopez molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT christianachoe molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT philippwnschmid molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT nicolasbloemeke molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT florianruhrnoßl molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT martinhaslbeck molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT juliaesservonbieren molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT michaelsattler molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT possuhuang molecularbasisofchaperonemediatedinterleukin23assemblycontrol AT matthiasjfeige molecularbasisofchaperonemediatedinterleukin23assemblycontrol |
| _version_ |
1718391080701919232 |