The Journal of Neuroscience, August 8, 2007, ():
Munc18-1: Sequential Interactions with the Fusion Machinery Stimulate Vesicle Docking and Priming
J. Neurosci. Gulyás-Kovács et al.
27: 8676
Supplemental Data
Files in this Data Supplement:
- supplemental material -
Supplemental Table
- supplemental material
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Suppl. Fig. 1. H-bonding of D34 in Munc18-1 is a conserved feature in SM proteins
(A) Details from the structural model of Munc18-1 (PDB code: 1DN1). D34 in red, predicted H-bonding partners are blue and H-bonds are green. (B) Multiple sequence alignments of SM proteins. Arrowheads point to D34 and the predicted interacting partners (S37, T78 and S83). The corresponding four residues in Sly1p are D59, S62, S103 and S108. (C) Structural detail in Sly1p (PDB code: 1MQS) showing these four residues. Note the N-terminal Sed5p peptide (purple) marking the hydrophobic syntaxin 1 binding pocket of Sly1p.
- supplemental material
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Suppl. Fig. 2. Functional characterization of the R39C mutation in Munc18-1.
Rescue of secretion in munc18-1 -/- cells by expressing Munc18-1 R39C (average of 56 cells). Munc18-1 was used as positive control (average of 55 cells).
