A Casein Kinase II Phosphorylation Site in the Cytoplasmic Domain of the Cation-dependent Mannose 6-Phosphate Receptor Determines the High Affinity Interaction of the AP-1 Golgi Assembly Proteins with Membranes
Open Access
- 1 January 1996
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 271 (4), 2171-2178
- https://doi.org/10.1074/jbc.271.4.2171
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Mannose 6-Phosphate Receptors and ADP-ribosylation Factors Cooperate for High Affinity Interaction of the AP-1 Golgi Assembly Proteins with MembranesJournal of Biological Chemistry, 1996
- Mechanisms of intracellular protein transportNature, 1994
- ARF: a key regulatory switch in membrane traffic and organelle structureCurrent Opinion in Cell Biology, 1994
- Signal-Dependent Membrane Protein Trafficking in the Endocytic PathwayAnnual Review of Cell Biology, 1993
- Biochemical dissection of AP-1 recruitment onto Golgi membranes.The Journal of cell biology, 1993
- The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding proteinCell, 1993
- Phosphorylation of the cation-independent mannose 6-phosphate receptor is closely associated with its exit from the trans-Golgi network.The Journal of cell biology, 1993
- A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chainsCell, 1992
- Quaternary structure of the Mr 46,000 mannose 6-phosphate specific receptor: effect of ligand, pH and receptor concentration on the equilibrium between dimeric and tetrameric receptor formsBiochemistry, 1990
- The trans Golgi Network: Sorting at the Exit Site of the Golgi ComplexScience, 1986