Recognition of a Basic AP-2 Binding Motif within the C2B Domain of Synaptotagmin Is Dependent on Multimerization

Synaptotagmin is a multifunctional membrane protein that may regulate exo-endocytic cycling of synaptic vesicles at the presynaptic plasmalemma. Its C2B domain has been postulated to interact with a variety of effector molecules including acidic phospholipids, phosphoinositides, SNAREs (soluble N-et...

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Veröffentlicht in:	The Journal of biological chemistry 2004-12, Vol.279 (52), p.54872-54880
Hauptverfasser:	Grass, Isabelle, Thiel, Stefanie, Höning, Stefan, Haucke, Volker
Format:	Artikel
Sprache:	eng
Schlagworte:	Adaptor Protein Complex 2 - genetics Adaptor Protein Complex 2 - metabolism Amino Acid Sequence Animals Binding Sites Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Cell Line Cell Membrane - metabolism Chemical Phenomena Chemistry, Physical Endocytosis Glutathione Transferase - genetics Membrane Glycoproteins - chemistry Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Molecular Sequence Data Mutagenesis Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism PC12 Cells Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Rats Recombinant Fusion Proteins Sequence Alignment Signal Transduction Structure-Activity Relationship Synaptotagmins Transfection
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