Journal article

The UBA domain of SnRK1 promotes activation and maintains catalytic activity

S Emanuelle, MS Doblin, PR Gooley, MS Gentry

Biochemical and Biophysical Research Communications | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2018

Abstract

Sucrose non-fermenting 1-related protein kinase 1 (SnRK1) is a central metabolic regulator and the plant orthologue of the mammalian AMP-activated protein kinase (AMPK); both are energy-sensing heterotrimeric enzymes comprising a catalytic α- and regulatory β- and γ-subunits. α-Subunits contain a serine/threonine kinase domain (KD) at their N-terminus that is immediately followed by a small regulatory domain termed the auto-inhibitory domain (AID) in AMPK and the ubiquitin-associated domain (UBA) in SnRK1. Association of the AID with the AMPK KD inhibits activating phosphorylation of the KD by upstream kinases and promotes dephosphorylation, as well as inhibiting AMPK catalytic activity. Des..

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University of Melbourne Researchers

Grants

Awarded by National Institute of Neurological Disorders and Stroke


Funding Acknowledgements

This work was supported by Kentucky Science and Energy Foundation [grants KSEF-2268RDE-014, KSEF-2971-RDE-017], National Science Foundation [grants IIA-1355438, MCB-1252345], Australian Research Council Centre of Excellence in Plant Cell Walls [grant CE1101007] and an Australia Research Council Discovery [grant DP110103161].