Identification of syntaxin 1A as a novel binding protein for presenilin-1

Stephanie K F Smith, Howard A. Anderson, Gang Yu, Alan G S Robertson, Shelley J. Allen, Sue J. Tyler, Ruth L. Naylor, Grant Mason, Gordon W. Wilcock, Paul A. Roche, Paul E. Fraser, David Dawbarn

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Mutations in the presenilin 1 gene have been shown to result in Alzheimer's disease. Presenilin 1 is a multi-transmembrane protein with a large hydrophilic loop near the C-terminus. This region is required for known functions of presenilin 1. We have constrained this loop within the active site of the bacterial protein, thioredoxin, to mimic its native conformational state. This hybrid protein was used as bait in a yeast two hybrid screen in an attempt to identify presenilin binding proteins. By this method syntaxin 1A, a synaptic plasma membrane protein, was identified as a novel binding protein for presenilin 1. In vitro experiments confirm the two-hybrid results suggesting that PS1 binds syntaxin under physiological conditions. Theme: Disorders of the nervous system. Topic: Degenerative disease: Alzheimer's - other. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)100-107
Number of pages8
JournalMolecular Brain Research
Issue number1-2
StatePublished - May 31 2000


  • Alzheimer's disease
  • Presenilin 1
  • Syntaxin
  • Thioredoxin

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience


Dive into the research topics of 'Identification of syntaxin 1A as a novel binding protein for presenilin-1'. Together they form a unique fingerprint.

Cite this