2009
DOI: 10.1074/jbc.m109.013508
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Abrogating Munc18-1-SNARE Complex Interaction Has Limited Impact on Exocytosis in PC12 Cells

Abstract: Neuronal communication relies on the fusion of neurotransmitter-containing vesicles with the plasma membrane. The soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) proteins initiate membrane fusion through the formation of the SNARE complex, a process tightly regulated by Sec1/Munc18-1 (SM) proteins. The emerging trend is that SM proteins promote SNARE-mediated membrane fusion by binding to a Syntaxin N-terminal motif. Here we report that mutations in the hydrophobic pocket … Show more

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Cited by 41 publications
(76 citation statements)
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“…Binding mode 2 is the major binding mode for the binary interaction between Munc18-1 and syntaxin-1A (15,25,45), whereas binding mode 1 alone cannot support the binary interaction but can further secure the binary interaction (20,25). For example, Munc18-1 and syntaxin-1A bind each other at low nanomolar concentrations even when the hydrophobic pocket of Munc18-1 is mutated or the N-peptide of syntaxin-1A is removed (25,31).…”
Section: Discussionmentioning
confidence: 99%
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“…Binding mode 2 is the major binding mode for the binary interaction between Munc18-1 and syntaxin-1A (15,25,45), whereas binding mode 1 alone cannot support the binary interaction but can further secure the binary interaction (20,25). For example, Munc18-1 and syntaxin-1A bind each other at low nanomolar concentrations even when the hydrophobic pocket of Munc18-1 is mutated or the N-peptide of syntaxin-1A is removed (25,31).…”
Section: Discussionmentioning
confidence: 99%
“…The lack of rescue by the hydrophobic pocket mutants in Munc18-2 is surprising, as we previously found that the expressions of Munc18-1 with the identical mutations showed 70-80% of the rescue ability compared with the wild type, using Munc18-1 KD and Munc18-1/2 DKD PC12 cells (15,31). Furthermore, the same (F115E) and a similar (L130K) mutant have shown a complete rescue ability in autaptic neurotransmission of Munc18-1-deficient neurons (32).…”
Section: Munc18-1 and Munc18-2 Can Effectively Support Mast Cell Degrmentioning
confidence: 99%
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“…SM proteins have also been shown to interact with SNARE binary and SNARE ternary complexes (9)(10)(11), and these interactions require an open Sx binding mode as well as the presence of an N-peptide, the 10-30 residues at the very N terminus of Sx (11)(12)(13)(14). The two binding modes (closed and N-peptide) are thought to be associated with different aspects of SM protein function.…”
mentioning
confidence: 99%
“…From examination of the literature, we noted that C-terminal anchoring of Sx may be important for Munc18a to play a positive role in SNARE-fusion regulation (Table 1). Using an in vitro pull-down assay, when Sx1a is immobilized via its C-terminus onto affinity beads, Munc18a can assemble the SNARE ternary complex, or bind to an already assembled SNARE ternary complex (Hu et al, 2011;Malintan et al, 2009). On the other hand, soluble Sx1a (1-262) that has a C-terminus free in solution was unable to form a SNARE complex in the presence of Munc18a (Burkhardt et al, 2008) (Table 1).…”
Section: The Effect Of the Sx C-terminusmentioning
confidence: 99%