Science exchange logo white
  • Solutions
      Buyers

      We are making R&D services readily available to every organization that seeks to make scientific impact. Learn More

      Providers

      We are changing the way providers access and engage customers to streamline the sale and delivery of R&D services. Learn More

      Industries Agriscience Animal Health Basic Research Biopharmaceutical Chemicals Consumer Health Food Science Medical Devices
      Reproducibility

      We believe that good experiments can and should be independently replicated and validated. Learn More

  • Resources
    Innovation Blog
    Customer Stories
    Events
    Industry Trends
    News
    Product Updates
    Help Center
  • About
    About
    Our Story
    Leadership
    Partners
    Join the Team
  • Contact
  • Log In Sign Up
  • Get a Demo
  • Interactions of the NPXY microdomains of the low density lipoprotein receptor-related protein 1.

    Proteomics. 9(22):5016-28. doi: 10.1002/pmic.200900457. November 2009. View on PubMed.
  • Authors

    Guttman M, Betts GN, Barnes H, Ghassemian M, van der Geer P, and Komives EA
  • Abstract

    The low density lipoprotein receptor-related protein 1 (LRP1) mediates internalization of a large number of proteins and protein-lipid complexes and is widely implicated in Alzheimer's disease. The cytoplasmic domain of LRP1 (LRP1-CT) can be phosphorylated by activated protein-tyrosine kinases at two NPXY motifs in LRP1-CT; Tyr 4507 is readily phosphorylated and must be phosphorylated before phosphorylation of Tyr 4473 occurs. Pull-down experiments from brain lysate revealed numerous proteins binding to LRP1-CT, but the results were highly variable. To separate which proteins bind to each NPXY motif and their phosphorylation dependence, each NPXY motif microdomain was prepared in both phosphorylated and non-phosphorylated forms and used to probe rodent brain extracts for binding proteins. Proteins that bound specifically to the microdomains were identified by LC-MS/MS, and confirmed by Western blot. Recombinant proteins were then tested for binding to each NPXY motif. The NPXY(4507) (membrane distal) was found to interact with a large number of proteins, many of which only bound the tyrosine-phosphorylated form. This microdomain also bound a significant number of other proteins in the unphosphorylated state. Many of the interactions were later confirmed to be direct with recombinant proteins. The NPXY(4473) (membrane proximal) bound many fewer proteins and only to the phosphorylated form.

Science exchange logo white

  • Facebook
  • Twitter
  • LinkedIn

Solutions

  • Buyers
  • Providers
  • Reproducibility

Industries

  • Agriscience
  • Animal Health
  • Basic Research
  • Biopharmaceutical
  • Chemicals
  • Consumer Health
  • Food Science
  • Medical Devices

Resources

  • Innovation Blog
  • Customer Stories
  • Events
  • Industry Trends
  • News
  • Product Updates

About

  • Our Story
  • Leadership
  • Partners
  • Join the Team

Support

  • Contact Us
  • Help Center
  • Trust
  • Terms of Use
  • Privacy Policy

Copyright © 2021 Science Exchange, Inc. All rights reserved.