Abstract
PRK1 is a member of the protein kinase C-related kinase (PRK) family of serine/threonine kinases and a downstream effector of Rho GTPases. PRK1 has three N-terminal Homology Region 1 (HR1) domains (HR1a, HR1b and HR1c), which form antiparallel coiled coils that interact with Rho family GTPases. PRK1 also has a C2-like domain that targets it to the plasma membrane and a kinase domain, which is a member of the protein kinase C superfamily. PRK1 is involved in cytoskeletal regulation, cell adhesion, cell cycle progression and the immune response, and is implicated in cancer. There is currently no structural information for the HR1c domain. The 1H, 15N and 13C NMR backbone and sidechain resonance assignment of the HR1c domain presented here forms the basis for this domain’s structural characterisation. This work will also enable studies of interactions between the three HR1 domains in an effort to obtain structural insight into the regulation of PRK1 activity.
Highlights
Transcriptional regulation (Metzger et al 2003, 2008), the immune response (Park et al 2016), cell cycle progression (Schmidt et al 2007), thromboxane signalling (O’Sullivan et al 2015) and mTOR signalling (Yang et al 2017; Wallroth et al 2019)
Protein kinase C-related kinase 1 (PRK1) has a C2-like domain, which targets the protein to the plasma membrane and a C-terminal catalytic domain, which belongs to the protein kinase C family
Small GTPases like RhoA and Rac1 can activate PRK1 activity (Amano et al 1996; Lu and Settleman 1999) and it is thought that RhoA binds to HR1a to relieve autoinhibition mediated by a pseudosubstrate region in this domain (Kitagawa et al 1996)
Summary
PRK1 has three N-terminal HR1 domains, HR1a, HR1b and HR1c. Small GTPases like RhoA and Rac can activate PRK1 activity (Amano et al 1996; Lu and Settleman 1999) and it is thought that RhoA binds to HR1a to relieve autoinhibition mediated by a pseudosubstrate region in this domain (Kitagawa et al 1996). We present the 1H, 15N and 13C NMR resonance assignment of the PRK1 HR1c domain This will form the basis for structure determination and for investigating interactions between the three PRK1 HR1 domains, providing much needed structural insight into PRK1 regulation
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