Identification of phosphorylation sites on NAP1/AZI2

By Dr WeiQiang Chen and Sascha Martens
View Published Dataset

Output Details

Description
We observed smearing for the TBK1-adaptor protein NAP1/AZI2 during mitophagy. To verify whether this smearing was due to phosphorylation by TBK1, we performed an in vitro kinase assay and complemented this with the immunoprecipitation of NAP1 from HAP1, whose genetic background (FIP200 knockout) results in hyperactivation of TBK1.
Tags
  • Mass spectrometry
Team
Team Hurley
Program
Collaborative Research Network
Theme
PD Functional Genomics

Meet the Authors

Related Research

Proteomics for STING KO and STINGRRAA RAW 264.7 macrophages

Using immunopeptidomics analysis we showed that STING regulates the repertoire of peptides displayed at the cell surface of macrophages during inflammation, highlighting a potential role in immunosurveillance and potential targets for therapy

View Dataset

Proteomic analysis of iNeurons lacking ER-phagy receptors

Proteomic analysis of iNeurons and cells lacking ER-phagy receptors FAM134C, FAM134A, FAM134B, TEX264, and CCPG1 showed distinct protein profiles, highlighting their roles in ER-phagy pathways.

View Dataset

Deficiency of the frontotemporal dementia gene GRN results in gangliosidosis.

Homozygous mutations of granulin precursor (GRN) lead to neuronal ceroid lipofuscinosis1, a severe neurodevelopmental disease, in humans and neuroinflammation in mice2. Haploinsufficiency of GRN almost invariably causes frontotemporal dementia…

View Article
View More Outputs
Aligning Science Across Parkinson's
Powered by  GDPR Cookie Compliance
Privacy Overview

This website uses cookies so that we can provide you with the best user experience possible. Cookie information is stored in your browser and performs functions such as recognising you when you return to our website and helping our team to understand which sections of the website you find most interesting and useful.