例如:"lncRNA", "apoptosis", "WRKY"

HUNK Phosphorylates Rubicon to Support Autophagy.

Int J Mol Sci. 2019 Nov 19;20(22)
Joelle N Zambrano 1 , Scott T Eblen 1 , Melissa Abt 2 , J Matthew Rhett 1 , Robin Muise-Helmericks 3 , Elizabeth S Yeh 2
Joelle N Zambrano 1 , Scott T Eblen 1 , Melissa Abt 2 , J Matthew Rhett 1 , Robin Muise-Helmericks 3 , Elizabeth S Yeh 2
+ et al

[No authors listed]

Author information
  • 1 Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC 29425, USA.
  • 2 Department of Pharmacology and Toxicology, Indiana University School of Medicine, Simon Cancer Center, Indianapolis, IN 46202, USA.
  • 3 Department of Regenerative Medicine and Cell Biology, Medical University of South Carolina, Charleston, SC 29425, USA.

摘要


BACKGROUND:Autophagy is a catabolic cellular recycling pathway that is essential for maintaining intracellular homeostasis. Autophagosome formation is achieved via the coordination of the Beclin-1 protein complex. Rubicon is a Beclin-1 associated protein that suppresses autophagy by impairing the activity of the class III PI3K, Vps34. However, very little is known about the molecular mechanisms that regulate Rubicon function. METHODS:In this study, co-immunoprecipitation and kinase assays were used to investigate the ability of Hormonally Upregulated Neu-associated Kinase (HUNK) to bind to and phosphorylate Rubicon. LC3B was monitored by immunofluorescence and immunoblotting to determine whether phosphorylation of Rubicon by HUNK controls the autophagy suppressive function of Rubicon. RESULTS:Findings from this study identify Rubicon as a novel substrate of HUNK and show that phosphorylation of Rubicon inhibits its function, promoting autophagy.

KEYWORDS: HUNK, Rubicon, autophagy, kinase, phosphorylation