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dc.contributor.authorLatham, Catherine F
dc.contributor.authorLopez, Jamie A
dc.contributor.authorhu, S-Hong Hu
dc.contributor.authorGee, Christine L
dc.contributor.authorWestbury, Elizabeth
dc.contributor.authorBlair, Duncan H
dc.contributor.authorArmishaw, Chris J
dc.contributor.authorAlewood, Paul F
dc.contributor.authorBryant, Nia J
dc.contributor.authorJames, David E
dc.contributor.authorMartin, Jennifer L
dc.date.accessioned2017-09-26T23:41:13Z
dc.date.available2017-09-26T23:41:13Z
dc.date.issued2006
dc.identifier.issn1398-9219
dc.identifier.doi10.1111/j.1600-0854.2006.00474.x
dc.identifier.urihttp://hdl.handle.net/10072/347543
dc.description.abstractSec1p/Munc18 (SM) proteins are believed to play an integral role in vesicle transport through their interaction with SNAREs. Different SM proteins have been shown to interact with SNAREs via different mechanisms, leading to the conclusion that their function has diverged. To further explore this notion, in this study, we have examined the molecular interactions between Munc18c and its cognate SNAREs as these molecules are ubiquitously expressed in mammals and likely regulate a universal plasma membrane trafficking step. Thus, Munc18c binds to monomeric syntaxin4 and the N-terminal 29 amino acids of syntaxin4 are necessary for this interaction. We identified key residues in Munc18c and syntaxin4 that determine the N-terminal interaction and that are consistent with the N-terminal binding mode of yeast proteins Sly1p and Sed5p. In addition, Munc18c binds to the syntaxin4/SNAP23/VAMP2 SNARE complex. Pre-assembly of the syntaxin4/Munc18c dimer accelerates the formation of SNARE complex compared to assembly with syntaxin4 alone. These data suggest that Munc18c interacts with its cognate SNAREs in a manner that resembles the yeast proteins Sly1p and Sed5p rather than the mammalian neuronal proteins Munc18a and syntaxin1a. The Munc18c–SNARE interactions described here imply that Munc18c could play a positive regulatory role in SNARE assembly.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherBlackwell Munksgaard
dc.relation.ispartofpagefrom1408
dc.relation.ispartofpageto1419
dc.relation.ispartofissue10
dc.relation.ispartofjournalTraffic
dc.relation.ispartofvolume7
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchMedical microbiology
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode3207
dc.titleMolecular dissection of the Munc18c/syntaxin4 interaction: Implications for regulation of membrane trafficking
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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