Functional studies for presynatic proteins which may control efficiency of synaptic transmission

控制突触传递效率的突前蛋白的功能研究

• 批准号: 14380369
• 负责人: MOCHIDA Sumiko
• 金额: $ 9.66万
• 依托单位: Tokyo Medical University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (B)
• 财政年份: 2002
• 资助国家: 日本
• 起止时间: 2002 至 2004
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-14380369/
• 关键词: synaptic transmission; presynaptic terminal proteins; Ca^<2+>; Calmodulin; Ca^<2+> channels; Ca^<2+>-binding protein; GTP-binding protein; Motor protein; sympathetic neurons in culture; シナプス; シナプス小胞; 燐酸化; アクティヴゾーン; リン酸化; 神経伝達物質; SNARE蛋白質

Neurotransmitter release is triggered by Ca^<2+> entered into presynaptic nerve terminals through voltage-dependent Ca^<2+> channels activated by an action potential. Recently, various proteins were found in presynaptic terminals. For example, SNARE proteins which form a core complex and involved in synaptic vesicle exocytosis, synaptic vesicle proteins or synaptic vesicle associated with Ca^<2+>sensor proteins, active zone cytomatrix proteins that also form a complex and motor proteins that may mobilize synaptic vesicles, and Ca^<2+> channel interacting proteins which may control Ca^<2+> channel activity.To examine possible roles of these proteins in regulation of synaptic transmission efficiency, we employed synapses formed between rat superior cervical ganglion neurons in long-term culture. We introduced exogenous synthesized peptides or, protein, or transfected cDNAs of a presynaptic protein and monitored changes in synaptic transmissionby recording excitatory postsynaptic potentials generated by presynaptic action potentials. We revealed a mechanism of regulation of SNARE complex formation by binding of Ca^<2+>/Calmodulin to syntaxin IA^<1)>, functional differences between three types of Ca^<2+> channels expressed in the brain^<2)> a possible role of cytomatrix proteins at the active zone^<3)>, regulation of exocytosis by SV2 binding to a Ca^<2+> sensor synaptotagmin^<4)>, regulation of exocytosis by G-protein βγ subunit binding to N-type Ca^<2+> channel^<5)>, regulation of synaptic vesicle trafficking by myosin IIB but not by IIA, Va or Vb (preparing for re-submission).

神经递质的释放是由Ca^<2+>通过电压依赖性CA^<2+>通道触发的Ca^<2+>启用。最近，在突触前末端发现了各种蛋白质。例如，形成核心复合物并参与突触囊泡外吞作用，合成囊泡蛋白或与CA^<2+>传感器蛋白相关的合成囊泡的核心蛋白这些蛋白质在调节突触传播效率中的作用，我们在长期培养中采用了大鼠超振神经神经元之间形成的突触。我们引入了外源合成Pepperides或蛋白质，蛋白质或蛋白质或翻译的cDNA，或者翻译的粘液蛋白前蛋白质的cDNA，并在突触传播效果上启用了portionsics portive seplesyn persynapts pressyn pressyn pressigys syplesyn pressigeds processyn portive sectients sysyn pressigeds syplesyn。我们揭示了一种通过Ca^<2+>/钙调蛋白与征毒素IA^<1）的结合来调节SNARE复合物形成的机制Synaptotagmin^<4）>，通过与N型Ca^<2+>通道^<5）结合的G蛋白βγ亚基调节外吞作用，肌球蛋白IIB对突触囊泡运输的调节，但不是IIA，VA或VB（准备重新提出）。

项目成果

Requirement for the synaptic protein interaction site for reconstitution of synaptic transmission by P/Q-type calcium channels

• DOI: 10.1073/pnas.262787699
• 发表时间: 2003-03-04
• 期刊: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• 影响因子: 11.1
• 作者: Mochida, S;Westenbroek, RE;Catterall, WA
• 通讯作者: Catterall, WA

持田澄子: "脳機能の解明 生命科学の主潮流"赤池紀扶. 570(9) (2002)

Sumiko Mochida：“大脑功能的阐明：生命科学的主要趋势”Norifu Akaike 570(9) (2002)。

G protein {beta}{gamma} subunits mediate presynaptic inhibition of transmitter release from rat superior cervical ganglion neurones in culture

G蛋白{β}{gamma}亚基介导培养的大鼠颈上神经节神经元递质释放的突触前抑制

• 发表时间: 2005
• 期刊: Journal of Physiology 563(Pt 3)
• 作者: Stephens GJ

Akihiro Ohyama: "Regulation of exocytosis through Ca^<2+> /ATP-dependent binding of autophosphorylated Ca^<2+>calmodulin-activated protein kinase II to syntaxin 1A"Journal of Neuroscience. 22・9. 3342-3351 (2002)

Akihiro Ohyama：“通过 Ca^2+/ATP 依赖性结合自磷酸化 Ca^2+ 钙调蛋白激活蛋白激酶 II 与突触蛋白 1A 的胞吐调节”神经科学杂志 22・9。 ）

Regulation of excytosis through Ca^<2+>/ATP-dependent binding of autophosphorylated Ca^<2+>/calmodulin-activated protein kinase II to syntaxin 1A

通过 Ca^2/ATP 依赖性自磷酸化 Ca^2/钙调蛋白激活蛋白激酶 II 与突触蛋白 1A 的结合调节胞吐作用

• 发表时间: 2002
• 期刊: Journal of Neuroscience 22
• 作者: Ohyama;A.
• 通讯作者: A.