Synapsin I is expressed in epithelial cells: Localization to a unique trans-Golgi compartment
| Autor: | E.R. Kolen, L. Braiterman, Anthony J. Baines, A.L. Hubbard, Fred S. Gorelick, R.I. Bustos |
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| Předmět: |
Male
Synapsin I Cytochalasin D Antineoplastic Agents Biology Vesicle tethering Rats Sprague-Dawley symbols.namesake Tubulin Myosin Mannosidases Animals Cytoskeleton Protein kinase A Transport Vesicles Cells Cultured Glycoproteins Brain Chemistry Myosin Type II Membrane Glycoproteins Nocodazole Membrane Proteins Epithelial Cells Cell Biology Golgi apparatus Synapsins Molecular biology Cell biology Rats Synaptic vesicle exocytosis nervous system symbols Hepatocytes Phosphorylation RNA trans-Golgi Network |
| Zdroj: | Scopus-Elsevier |
| Popis: | Synapsin I is abundant in neural tissues. Its phosphorylation is thought to regulate synaptic vesicle exocytosis in the pre-synaptic terminal by mediating vesicle tethering to the cytoskeleton. Using anti-synapsin antibodies, we detected an 85 kDa protein in liver cells and identified it as synapsin I. Like brain synapsin I, non-neuronal synapsin I is phosphorylated in vitro by protein kinase A and yields identical 32P-peptide maps after limited proteolysis. We also detected synapsin I mRNA in liver by northern blot analysis. These results indicate that the expression of synapsin I is more widespread than previously thought. Immunofluorescence analysis of several non-neuronal cell lines localizes synapsin I to a vesicular compartment adjacent to trans-elements of the Golgi complex, which is also labeled with antibodies against myosin II; no sub-plasma membrane synapsin I is evident. We conclude that synapsin I is present in epithelial cells and is associated with a trans-Golgi network-derived compartment; this localization suggests that it plays a role in modulating post-TGN trafficking pathways. |
| Databáze: | OpenAIRE |
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