Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation

In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with t...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2013-07, Vol.110 (31), p.12637-12642
Hauptverfasser: Colbert, Karen N., Hattendorf, Douglas A., Weiss, Thomas M., Burkhardt, Pawel, Fasshauer, Dirk, Weis, William I.
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container_issue 31
container_start_page 12637
container_title Proceedings of the National Academy of Sciences - PNAS
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creator Colbert, Karen N.
Hattendorf, Douglas A.
Weiss, Thomas M.
Burkhardt, Pawel
Fasshauer, Dirk
Weis, William I.
description In neurons, soluble N -ethylmaleimide–sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1–24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1aΔN), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1aΔN, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a–Syx1a complex.
doi_str_mv 10.1073/pnas.1303753110
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We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a–Syx1a complex.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>23858467</pmid><doi>10.1073/pnas.1303753110</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
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subjects Amino Acid Substitution
Amino acids
BASIC BIOLOGICAL SCIENCES
Biological Sciences
Cell membranes
Crystal structure
Electron density
Evolutionary linguistics
Exocytosis
Humans
Hydrogen bonds
membrane fusion
membrane trafficking
Munc18 Proteins - chemistry
Munc18 Proteins - genetics
Munc18 Proteins - metabolism
Mutation
Neurons
Peptides
plasma membrane
Protein Binding
protein crystallography
Protein Structure, Quaternary
Protein Structure, Secondary
Proteins
Sequence Deletion
SM proteins
SNARE proteins
SNARE Proteins - chemistry
SNARE Proteins - genetics
SNARE Proteins - metabolism
synaptic vesicles
Syntaxin 1 - chemistry
Syntaxin 1 - genetics
Syntaxin 1 - metabolism
X-radiation
X-ray diffraction
title Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation
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