Interactions among the SNARE proteins and complexin analyzed by a yeast four-hybrid assay
| Autor: | Alvin M. Shih, Ok Ho Shin |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Vesicle fusion
Synaptobrevin STX1A Chemistry Biophysics Nerve Tissue Proteins Munc-18 Cell Biology Biochemistry Synaptotagmin 1 Cell biology Adaptor Proteins Vesicular Transport Complexin Two-Hybrid System Techniques SNAP23 biological phenomena cell phenomena and immunity SNARE Proteins SNARE complex Molecular Biology Protein Binding |
| Zdroj: | Analytical Biochemistry. 416:107-111 |
| ISSN: | 0003-2697 |
| Popis: | Exocytosis is one of the most crucial and ubiquitous processes in all of biology. This event is mediated by the formation of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complexes, ternary assemblies of syntaxin, SNAP23/SNAP25 (synaptosomal-associated protein of 23 or 25 kDa), and synaptobrevin. The exocytotic process can be further regulated by complexin, which interacts with the SNARE complex. Complexin is involved in a Ca(2+)-triggered exocytotic process. In eukaryotic cells, multiple isoforms of SNARE proteins are expressed and are involved in distinct types of exocytosis. To understand the underlying biochemical mechanism of various exocytotic processes mediated by different SNARE protein isoforms, we systematically analyzed the interactions among syntaxin, SNAP23/SNAP25, synaptobrevin, and complexin by employing a newly developed yeast four-hybrid interaction assay. The efficiency of SNARE complex formation and the specificity of complexin binding are regulated by the different SNARE protein isoforms. Therefore, various types of exocytosis, occurring on different time scales with different efficiencies, can be explained by the involved SNARE complexes composed of different combinations of SNARE protein isoforms. |
| Databáze: | OpenAIRE |
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