Competition between members of the tribbles pseudokinase protein family shapes their interactions with mitogen activated protein kinase pathways.

ABSTRACT: Spatio-temporal regulation of intracellular signalling networks is key to normal cellular physiology; dysregulation of which leads to disease. The family of three mammalian tribbles proteins has emerged as an important controller of signalling via regulating the activity of mitogen activated protein kinases (MAPK), the PI3-kinase induced signalling network and E3 ubiquitin ligases. However, the importance of potential redundancy in the action of tribbles and how the differences in affinities for the various binding partners may influence signalling control is currently unclear. We report that tribbles proteins can bind to an overlapping set of MAPK-kinases (MAPKK) in live cells and dictate the localisation of the complexes. Binding studies in transfected cells reveal common regulatory mech

SUBMITTER: Guan H 

PROVIDER: S-EPMC5013389 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature