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, Ann Louise Hubbard

Research output: Contribution to journalArticle

Abstract

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
Volume114
Issue number20
StatePublished - 2001
Externally publishedYes

Fingerprint

Synapsins
Epithelial Cells
Myosin Type II
trans-Golgi Network
Synaptic Vesicles
Liver
Exocytosis
Presynaptic Terminals
Golgi Apparatus
Cyclic AMP-Dependent Protein Kinases
Cytoskeleton
Northern Blotting
Proteolysis
Fluorescent Antibody Technique
Anti-Idiotypic Antibodies
Phosphorylation
Cell Membrane

Keywords

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

ASJC Scopus subject areas

  • Cell Biology

Cite this

Bustos, R., Kolen, E. R., Braiterman, L., Baines, A. J., Gorelick, F. S., & Hubbard, A. L. (2001). Synapsin I is expressed in epithelial cells: Localization to a unique trans-Golgi compartment. Journal of Cell Science, 114(20), 3695-3704.

Synapsin I is expressed in epithelial cells : Localization to a unique trans-Golgi compartment. / Bustos, R.; Kolen, E. R.; Braiterman, L.; Baines, A. J.; Gorelick, F. S.; Hubbard, Ann Louise.

In: Journal of Cell Science, Vol. 114, No. 20, 2001, p. 3695-3704.

Research output: Contribution to journalArticle

Bustos, R, Kolen, ER, Braiterman, L, Baines, AJ, Gorelick, FS & Hubbard, AL 2001, 'Synapsin I is expressed in epithelial cells: Localization to a unique trans-Golgi compartment', Journal of Cell Science, vol. 114, no. 20, pp. 3695-3704.
Bustos, R. ; Kolen, E. R. ; Braiterman, L. ; Baines, A. J. ; Gorelick, F. S. ; Hubbard, Ann Louise. / Synapsin I is expressed in epithelial cells : Localization to a unique trans-Golgi compartment. In: Journal of Cell Science. 2001 ; Vol. 114, No. 20. pp. 3695-3704.
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AU - Gorelick, F. S.

AU - Hubbard, Ann Louise

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N2 - 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.

AB - 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.

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