pCAG-MBP-ATG9-Q835A

By Xuefeng Ren, PhD
View Published Lab Material

Output Details

Description
Expresses human ATG9-Q835A mutant in mammalian cells
Tags
  • Autophagy
  • Human
  • Protein purification
  • Recombinant
Team
Team Hurley
Program
Collaborative Research Network
Theme
PD Functional Genomics

Meet the Authors

  • User avatar fallback logo

    Xuefeng Ren, PhD

    Key Personnel: Team Hurley, 

    University of California, Berkeley

Related Research

A lipid transfer-dependent feedback loop activates ATG9A compartments in autophagy initiation

Phagophore formation requires ATG9, ATG2 and PI3KC3-C1. Authors show that ATG2 is crucial for PI3P appearance on ATG9A compartments with little PI, suggesting a lipid transfer-driven feedback loop supporting lipid transfer and ATG8 lipidation.

View Article

Autophagic stress activates distinct compensatory secretory pathways in neurons

Neurodegenerative diseases are linked to autophagy dysfunction causing harmful build-up of cellular waste. Neurons with Parkinson's mutation increase release of autophagic vesicles and exosomes, suggesting a protective response to chronic stress.

View Article

The human autophagy-initiating complexes ULK1C and PI3KC3-C1

ULK1C and PI3KC3-C1 are crucial for macroautophagy initiation. Recent research focuses on their structural organization, activation mechanisms, and roles in autophagy initiation's protein interaction network for potential therapeutic targeting.

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.