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Syntaxin clusters at secretory granules in a munc18-bound conformation
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.ORCID iD: 0000-0002-9442-3359
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.ORCID iD: 0000-0001-8893-7348
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2018 (English)In: Molecular Biology of the Cell, ISSN 1059-1524, E-ISSN 1939-4586, Vol. 29, no 22, p. 2700-2708Article in journal (Refereed) Published
Abstract [en]

Syntaxin (stx)-1 is an integral plasma membrane protein that is crucial for two distinct steps of regulated exocytosis, docking of secretory granules at the plasma membrane and membrane fusion. During docking, stx1 clusters at the granule docking site, together with the S/M protein munc18. Here we determined features of stx1 that contribute to its clustering at granules. In live insulin-secreting cells, stx1 and stx3 (but not stx4 or stx11) accumulated at docked granules, and stx1 (but not stx4) rescued docking in cells expressing botulinum neurotoxin-C. Using a series of stx1 deletion mutants and stx1/4 chimeras, we found that all four helical domains (Ha, Hb, Hc, SNARE) and the short N-terminal peptide contribute to recruitment to granules. However, only the Hc domain confers specificity, and it must be derived from stx1 for recruitment to occur. Point mutations in the Hc or the N-terminal peptide designed to interfere with binding to munc18-1 prevent stx1 from clustering at granules, and a mutant munc18 deficient in binding to stx1 does not cluster at granules. We conclude that stx1 is recruited to the docking site in a munc18-1-bound conformation, providing a rationale for the requirement for both proteins for granule docking.

Place, publisher, year, edition, pages
2018. Vol. 29, no 22, p. 2700-2708
National Category
Cell and Molecular Biology
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URN: urn:nbn:se:uu:diva-375859DOI: 10.1091/mbc.E17-09-0541ISI: 000455641000013PubMedID: 30156474OAI: oai:DiVA.org:uu-375859DiVA, id: diva2:1285099
Funder
Swedish Research CouncilSwedish Child Diabetes FoundationSwedish Diabetes AssociationThe Swedish Brain FoundationNovo NordiskGöran Gustafsson Foundation for Research in Natural Sciences and MedicineErnfors FoundationSwedish Society of MedicineAvailable from: 2019-02-01 Created: 2019-02-01 Last updated: 2019-02-01Bibliographically approved

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Yin, PengGandasi, Nikhil R.Arora, SwatiOmar-Hmeadi, MuhmmadSaras, JanBarg, Sebastian

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