While control of disorder of proteins plays a crucial role in the physiology of cells, we do not understand how cells guard the transitions between different phases of intrinsically disordered proteins (IDPs), liquid, gel or amyloid. A striking finding in recent years is that nuclear transport factors can protect against toxicity from disease-related IDPs. Vice versa, chaperones have been found to act on nuclear transport. With a consortium of experts on the nuclear pore complex, chaperones and aggregation pathology, we aim to elucidate how nuclear transport receptors and chaperones act as guardians of IDPs to ensure proper nuclear pore complex function and to protect against pathological aggregation. With this consortium, we are in a unique position to make a crucial step forward as we can address the problem through a complementary set of in silico, in vitro, and in vivo approaches. The knowledge obtained is expected to be vital to the understanding of neurodegenerative diseases caused by IDPs.