دورية أكاديمية
Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cells.
| العنوان: | Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cells. |
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| المؤلفون: | Malintan NT; Queensland Brain Institute and School of Biomedical Sciences, University of Queensland, Brisbane, Queensland 4072, Australia., Nguyen TH, Han L, Latham CF, Osborne SL, Wen PJ, Lim SJ, Sugita S, Collins BM, Meunier FA |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2009 Aug 07; Vol. 284 (32), pp. 21637-46. Date of Electronic Publication: 2009 May 29. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Munc18 Proteins/*physiology , SNARE Proteins/*metabolism, Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Calcium/metabolism ; Exocytosis ; Models, Biological ; Molecular Conformation ; Molecular Sequence Data ; PC12 Cells ; Protein Structure, Tertiary ; Qa-SNARE Proteins/metabolism ; Rats ; Recombinant Proteins/chemistry |
| مستخلص: | 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 of Munc18-1 (F115E and E132A), predicted to disrupt the N-terminal Sx1a interaction have a modest effect on binding to Sx1a in its free state, but abolish binding to the SNARE complex. Overexpression of the Munc18-1 mutant in PC12 cells lacking Munc18-1 rescues both neuroexocytosis and the plasma membrane localization of Syntaxin. However, total internal reflection fluorescence microscopy analysis reveals that expression of a Munc18-1 double mutant reduces the rate of vesicle fusion, an effect only detectable at the onset of stimulation. The Munc18-1 hydrophobic pocket is therefore critical for SNARE complex binding. However, mutations abrogating this interaction have a limited impact on Ca(2+)-dependent exocytosis in PC12 cells. |
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| المشرفين على المادة: | 0 (Munc18 Proteins) 0 (Qa-SNARE Proteins) 0 (Recombinant Proteins) 0 (SNARE Proteins) 0 (Stxbp1 protein, rat) SY7Q814VUP (Calcium) |
| تواريخ الأحداث: | Date Created: 20090602 Date Completed: 20090928 Latest Revision: 20211020 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC2755887 |
| DOI: | 10.1074/jbc.M109.013508 |
| PMID: | 19483085 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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| DOI: | 10.1074/jbc.M109.013508 |