Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25 Journal Article

  


Authors: Veit, M.; Söllner, T. H.; Rothman, J. E.
Article Title: Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
Abstract: Synaptotagmin, a likely calcium sensor for synaptic transmission, and SNAP-25, a t-SNARE of the presynaptic plasma membrane, are key proteins for the docking and fusion of synaptic and other vesicles. We report that both synaptotagmin and SNAP-25 are palmitoylated with their fatty acids attached in a labile thioester-type bond. A SNAP-25 mutant with deleted palmitoylation sites is found exclusively in the cytosol after cell fractionation, whereas the palmitoylated form of SNAP-25 is membrane-bound, establishing that SNAP-25 is membrane-anchored via covalently linked palmitate.
Keywords: controlled study; nonhuman; animal cell; protein binding; membrane protein; nerve cell; synaptotagmin; protein lipid interaction; palmitoylation; neurotransmission; syntaxin; palmitic acid; snare; priority journal; article; snap-25
Journal Title: FEBS Letters
Volume: 385
Issue: 1-2
ISSN: 0014-5793
Publisher: Wiley Blackwell  
Date Published: 1996-04-29
Start Page: 119
End Page: 123
Language: English
DOI: 10.1016/0014-5793(96)00362-6
PUBMED: 8641455
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-18244432240&doi=10.1016%2f0014-5793%2896%2900362-6&partnerID=40&md5=8303654906e091501dde949b263f87bd
Notes: Article -- Export Date: 22 November 2017 -- Source: Scopus
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MSK Authors
  1. Thomas H Sollner
    65 Sollner
  2. James E Rothman
    120 Rothman
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