Synaptotagmin restores kinetic properties of a syntaxin-associated N-type voltage sensitive calcium channel

Ofer Wiser, Dror Tobi, Michael Trus, Daphne Atlas

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

The voltage sensitive N-type calcium channel interacts functionally and biochemically with synaptotagmin (p65). N-type channel interaction with p65 is demonstrated in the Xenopus oocyte expression system, where p65 alters the steady state voltage inactivation of the N-channel, and fully restores the syntaxin-modified current amplitude and inactivation kinetics in a calcium dependent manner. In agreement with the functional results, GST-p65 fusion protein binds to a cytosolic region, amino acids 710-1090 of the N-type channel (N-loop710-1090). The results of the combined approach provide a functional and biochemical basis for proposing that p65 interaction with the N-type channel brings p65 into a close association with a syntaxin-coupled channel. In turn, calcium entry through the liberated channel initiates fusion of the primed vesicles with the cell membrane at a short distance from the site of calcium entry.

Original languageEnglish
Pages (from-to)203-207
Number of pages5
JournalFEBS Letters
Volume404
Issue number2-3
DOIs
StatePublished - 10 Mar 1997
Externally publishedYes

Keywords

  • N-type calcium channel
  • SNAP-25
  • Synaptotagmin
  • Syntaxin
  • Transmitter release

Fingerprint

Dive into the research topics of 'Synaptotagmin restores kinetic properties of a syntaxin-associated N-type voltage sensitive calcium channel'. Together they form a unique fingerprint.

Cite this