Bustos, R.I. and Kolen, E.R. and Braiterman, L. and Baines, Anthony J. and Gorelick, F.S. and Hubbard, A.L. (2001) Synapsin I is Expressed in Epithelial Cells: Localization to a Unique Trans-Golgi Compartment. Journal of Cell Science, 114 (20). pp. 3695-3704. ISSN 0021-9533. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
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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, non-neuronal synapsin I is phosphorylated in vitro by protein kinase A and yields identical (32)P-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 > Sciences > School of Biosciences > Cell & Developmental Biology Group|
|Depositing User:||Anthony Baines|
|Date Deposited:||02 Nov 2008 19:38 UTC|
|Last Modified:||27 Jun 2014 13:34 UTC|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/8636 (The current URI for this page, for reference purposes)|