Tyrosine Phosphorylation of the β2 Subunit of Clathrin Adaptor Complex AP-2 Reveals the Role of a Di-leucine Motif in the Epidermal Growth Factor Receptor Trafficking
Open Access
- 1 October 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (44) , 43411-43417
- https://doi.org/10.1074/jbc.m306072200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Molecular Architecture and Functional Model of the Endocytic AP2 ComplexCell, 2002
- Biological Basket Weaving: Formation and Function of Clathrin-Coated VesiclesAnnual Review of Cell and Developmental Biology, 2001
- Three ways to make a vesicleNature Reviews Molecular Cell Biology, 2000
- Phosphoinositide–Ap-2 Interactions Required for Targeting to Plasma Membrane Clathrin-Coated PitsThe Journal of cell biology, 1999
- A Structural Explanation for the Binding of Multiple Ligands by the α-Adaptin Appendage DomainCell, 1999
- A Structural Explanation for the Recognition of Tyrosine-Based Endocytotic SignalsScience, 1998
- Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding siteThe EMBO Journal, 1998
- Medium Chains of Adaptor Complexes AP-1 and AP-2 Recognize Leucine-based Sorting Signals from the Invariant ChainJournal of Biological Chemistry, 1998
- The α Chain of the AP-2 Adaptor Is a Clathrin Binding SubunitJournal of Biological Chemistry, 1995
- The role of clathrin, adaptors and dynamin in endocytosisCurrent Opinion in Cell Biology, 1994