Preserving protein function through reversible aggregation

Nature Cell Biology 19, 1142 (2017).
doi:10.1038/ncb3620

Author: Jörg Höhfeld
It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase triggers reversible aggregation to preserve protein function under stress.

Source: Nature Cell Biology - September 29, 2017 Category: Cytology Authors: J ö rg H ö hfeld Tags: News and Views Source Type: research