Publications by authors named "Carolin J Klose"
Article Synopsis
- The proper function of secreted proteins often relies on their correct assembly into complex structures, but cells struggle to differentiate between unassembled and misfolded proteins.
- The study focuses on how chaperones manage the assembly of interleukin 23 (IL-23), revealing that its α-subunit remains partially unstructured until it pairs with the β-subunit, indicating a site of incomplete folding.
- Different chaperones recognize this incomplete folding at several checkpoints during the secretory process, allowing for regulated assembly and showing that adjustments to chaperone recognition can lead to the successful secretion of functional IL-23.
The integrated stress response (ISR) tunes the rate of protein synthesis. Control is exerted by phosphorylation of the general translation initiation factor eIF2. eIF2 is a guanosine triphosphatase that becomes activated by eIF2B, a two-fold symmetric and heterodecameric complex that functions as eIF2's dedicated nucleotide exchange factor.
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