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Journal of Cell Science 114, 3695-3704 (2001)
© 2001 The Company of Biologists Limited

RESEARCH ARTICLE

Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment

Rodrigo Bustos1,*, E. Robert Kolen1,*, Lelita Braiterman1, Anthony J. Baines2, Fred S. Gorelick3 and Ann L. Hubbard3,{ddagger}

1 Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2105, USA
2 Biological Laboratory, University of Kent, Kent, CT2 7NJ, UK
3 Division of Gastroenterology, Department of Medicine, Yale University School of Medicine, West Haven, CT 06516, USA
* These authors contributed equally to this work

{ddagger}Author for correspondence (e-mail: alh{at}jhmi.edu)

Accepted June 26, 2001

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.

Key words: Synapsin I, Vesicular traffic, Epithelial cells, trans-Golgi network, Myosin II


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© The Company of Biologists Ltd 2001