Papers are like buses... You wait for ages, then two come along at once.
Huge congrats to @bornanovak.bsky.social and @jefflotthammer.bsky.social for pushing and driving every aspect of this work, preprinted ~1 year ago to the day (Friday before BPS), now published!
www.nature.com/articles/s41...
Couldn't have done it without an exciting collaboration with Julie Forman-Kay, Alan Moses, Olena Zhulyn and @johnrubinstein.bsky.social!
PRRC2A, PRRC2B and PRRC2C proteins link stress granule proteins to key regulators involved in selective translation, offering an insight to how stress granules may help with stress-induced translation reprogramming.
Using integrative quantitative proteomics, genetics, cell biology, and structural modeling, we demonstrate that PRRC2 proteins directly associate with the eIF3 complex, important for translation initiation.
These proteins (PRRC2A, PRRC2B, and PRRC2C) are intrinsically disordered proteins with no stable structure. By integrating functional proteomics with structural modeling, we found an effective strategy to define the functions of intrinsically disordered proteins in dynamic cellular processes.
Preprint alert!
Stress granules form rapidly under stress, when translation shuts down. What stress granule proteins do under basal condition remained a mysterious. Here, we identified stress granule proteins, PRRC2A, PRRC2B, and PRRC2C, as novel regulators of translation. Work by Jie Qi Huang.
