Direct interaction between SNAP-23 and L-type Ca²⁺channel Journal Articles

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abstract

During secretion, membrane-bound secretory vesicles dock and fuse at the base of porosomes in the cell plasma membrane. Among other proteins, the porosome is composed of SNAREs and Ca2+-channels. Ca2+-channels and SNAREs have been implicated in cell secretion. Several immunoprecipitation and binding studies suggest the physical interaction of the t-SNARE proteins, Syntaxin-1 and SNAP-25 with various Ca2+-channels. In this study, using yeast two-hybrid and immunoanalysis, we demonstrate for the first time, direct interaction of SNAP-23 and a L-type Ca2+-channel at the plasma membrane in pancreas.

authors

Cho, Won Jin
Jeremic, Aleksandar
Jena, Bhanu P

status

published

publication date

April 2005

has subject area

0304 Medicinal and Biomolecular Chemistry (FoR)
0601 Biochemistry and Cell Biology (FoR)
1103 Clinical Sciences (FoR)
Amino Acid Sequence (MeSH)
Animals (MeSH)
Base Sequence (MeSH)
Biochemistry & Molecular Biology (Science Metrix)
Calcium Channels, L-Type (MeSH)
Carrier Proteins (MeSH)
Cell Membrane (MeSH)
Immunoprecipitation (MeSH)
Male (MeSH)
Models, Molecular (MeSH)
Pancreas (MeSH)
Protein Binding (MeSH)
Qb-SNARE Proteins (MeSH)
Qc-SNARE Proteins (MeSH)
Rats (MeSH)
Rats, Sprague-Dawley (MeSH)
Sequence Homology, Amino Acid (MeSH)
Sequence Homology, Nucleic Acid (MeSH)
Two-Hybrid System Techniques (MeSH)
Yeasts (MeSH)

published in

Journal of Cellular and Molecular Medicine Journal