While most proteins neatly fold into stable structures, there are also many important proteins that are supposed to stay disordered. Disordered proteins can however be sticky and may clump together causing cellular dysfunction and, eventually, disease. An essential structure that relies disordered proteins is the Nuclear Pore Complex, the transport system acting as a selective barrier to the cell’s nucleus. In a joint effort, researchers from BSCS and ERIBA now show that a chaperone can safeguard the disordered proteins from the Nuclear Pore Complex to prevent them from aggregating together.
Kuiper et al, Nature Cell Biology 27-10-2022 The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis.
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