Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Phosphorylation of the ap2 mu subunit by aak1 mediates high affinity binding to membrane protein sorting signals

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Ricotta, D.
  • Conner, S. D.
  • Schmid, Sandra
  • von Figura, K.
  • Honing, S.

publication date

  • March 2002

journal

  • Journal of Cell Biology  Journal

abstract

  • During receptor-mediated endocytosis, AP2 complexes act as a bridge between the cargo membrane proteins and the clathrin coat by binding to sorting signals via the mu 2 subunit and to clathrin via the beta subunit. Here we show that binding of AP2 to sorting signals in vitro is regulated by phosphorylation of the mu 2 subunit of AP2. Phosphorylation of mu 2 enhances the binding affinity of AP2 for sorting motifs as much as 25-fold compared with dephosphorylated AP2. The recognition of sorting signals was not affected by the phosphorylation status of the alpha or beta 2 subunit, suggesting that phosphorylation of mu 2 is critical for regulation of AP2 binding to sorting signals. Phosphorylation of mu 2 occurs at a single threonine residue (Thr-156) and is mediated by the newly discovered adaptor-associated kinase, AAK1, which copurifies with AP2. We propose that phosphorylation of the AP2 mu 2 subunit by AAK1 ensures high affinity binding of AP2 to sorting signals of cargo membrane proteins during the initial steps of receptor-mediated endocytosis.

subject areas

  • Adaptor Protein Complex 2
  • Adaptor Proteins, Vesicular Transport
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Cell Membrane
  • Endocytosis
  • Membrane Proteins
  • Phosphorylation
  • Protein Serine-Threonine Kinases
  • Protein Transport
  • Receptors, Cell Surface
  • Swine
scroll to property group menus

Research

keywords

  • clathrin
  • coated vesicle
  • endocytosis
  • receptor
  • trafficking
scroll to property group menus

Identity

PubMed Central ID

  • PMC2173304

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200111068

PubMed ID

  • 11877457
scroll to property group menus

Additional Document Info

start page

  • 791

end page

  • 795

volume

  • 156

issue

  • 5

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support