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- W2052023774 abstract "Synaptotagmin 1 (Syt1) is a Ca2+ sensor for SNARE-mediated, Ca2+-triggered synaptic vesicle fusion in neurons. It is composed of luminal, transmembrane, linker, and two Ca2+-binding (C2) domains. Here we describe expression and purification of full-length mammalian Syt1 in insect cells along with an extensive biochemical characterization of the purified protein. The expressed and purified protein is properly folded and has increased α-helical content compared to the C2AB fragment alone. Post-translational modifications of Syt1 were analyzed by mass spectrometry, revealing the same modifications of Syt1 that were previously described for Syt1 purified from brain extract or mammalian cell lines, along with a novel modification of Syt1, tyrosine nitration. A lipid binding screen with both full-length Syt1 and the C2AB fragments of Syt1 and Syt3 isoforms revealed new Syt1–lipid interactions. These results suggest a conserved lipid binding mechanism in which Ca2+-independent interactions are mediated via a lysine rich region of the C2B domain while Ca2+-dependent interactions are mediated via the Ca2+-binding loops." @default.
- W2052023774 created "2016-06-24" @default.
- W2052023774 creator A5001967033 @default.
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- W2052023774 creator A5041683996 @default.
- W2052023774 creator A5076307322 @default.
- W2052023774 date "2011-10-26" @default.
- W2052023774 modified "2023-09-27" @default.
- W2052023774 title "Post-Translational Modifications and Lipid Binding Profile of Insect Cell-Expressed Full-Length Mammalian Synaptotagmin 1" @default.
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- W2052023774 doi "https://doi.org/10.1021/bi200998y" @default.
- W2052023774 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3217305" @default.
- W2052023774 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21928778" @default.
- W2052023774 hasPublicationYear "2011" @default.
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