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

R. Bustos, E. R. Kolen, L. Braiterman, A. J. Baines, F. S. Gorelick, A. L. Hubbard

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


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 suggest that it plays a role in modulating post-TGN trafficking pathways.

Original languageEnglish (US)
Pages (from-to)3695-3704
Number of pages10
JournalJournal of cell science
Issue number20
StatePublished - 2001
Externally publishedYes


  • Epithelial cells
  • Myosin II
  • Synapsin I
  • Trans-Golgi network
  • Vesicular traffic

ASJC Scopus subject areas

  • Cell Biology


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