Disruption of syntaxin-mediated protein interactions blocks neurotransmitter secretion

V. OConnor; C. Heuss; W. M. De Bello

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Disruption of syntaxin-mediated protein interactions blocks neurotransmitter secretion

机译：破坏语法蛋白介导的蛋白质相互作用可阻断神经递质的分泌

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The membrane protein syntaxin participates in several protein-protein interactions that have been impli- cated in neurotransmitter release. To probe the physiological importance of these interactions, we microinjected into the squid giant presynaptic terminal botulinum toxin C1, which cleaves syntaxin, and the H3 domain of syntaxin, which mediates binding to other proteins. Both reagents inhibited synaptic transmission yet did not affect the number or dis- tribution of synaptic vesicles at the presynaptic active zone. Recombinant H3 domain inhibited the interactions between syntaxin and SNAP-25 that underlie the formation of stable SNARE complexes in vitro. These data support the notion that syntaxin-mediated SNARE complexes are necessary for docked synaptic vesicles to fuse.

机译：膜蛋白语法蛋白参与神经递质释放中暗示的几种蛋白-蛋白相互作用。为了探究这些相互作用的生理重要性，我们将鱿鱼巨大的突触前终末肉毒杆菌毒素C1微注射到了语法素中，而语法素的H3域则注射了它与其他蛋白质的结合。两种试剂均抑制突触传递，但不影响突触前活性区的突触小泡的数量或分布。重组H3域抑制了语法素和SNAP-25之间的相互作用，这是体外稳定SNARE复合物形成的基础。这些数据支持以下观点：语法对接的SNARE复合物对于停靠的突触小泡融合是必需的。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1997年第22期|p.12186-12191|共6页
作者
V. OConnor; C. Heuss; W. M. De Bello;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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Disruption of syntaxin-mediated protein interactions blocks neurotransmitter secretion

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