Bustos, R.I. and Kolen, E.R. and Gorelick, F.S. and Baines, A.J. and Hubbard, A.L. (1999) Identification of synapsin I in epithelial cells. Molecular Biology of the Cell, 10 . 218A--218A. ISSN 1059-1524. (The full text of this publication is not available from this repository)
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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, nonneuronal 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.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||M. Nasiriavanaki|
|Date Deposited:||02 Jul 2009 08:15|
|Last Modified:||02 Jul 2009 08:15|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/17161 (The current URI for this page, for reference purposes)|