De ‐RSKing ERK – regulation of ERK1/2‐RSK dissociation by phosphorylation within a disordered motif

The protein kinases ERK1/2 and RSK associate in unstimulated cells but must separate to target other substrates. In this issue, Gógl et al. show that phosphorylation of RSK by active ERK1/2 culminates in the formation of an intramolecular charge clamp between Lys729 and the phosphate group on Ser732. This promotes the dissociation of ERK1/2 from RSK allowing them to engage with other targets.

Source: FEBS Journal - January 8, 2018 Category: Research Authors: Andrew M. Kidger, Simon J. Cook Tags: Commentary Source Type: research