Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila.
Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila.
复制标题
轴突运输运动驱动蛋白的突变增强了果蝇的麻痹并抑制了 Shaker。
DOI：
10.1093/genetics/142.1.195
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发表时间：
1996
期刊：
影响因子：
3.3
通讯作者：
Saxton,WM
中科院分区：
文献类型：
--
作者：
Hurd,DD;Stern,M;Saxton,WM
为了研究驱动蛋白转运携带离子通道活性所必需的蛋白质的囊泡的可能性，使用已建立的测试在果蝇中比较了驱动蛋白（Khc）和离子通道突变的影响。我们的研究结果表明，Khc突变产生的缺陷和遗传相互作用的特点麻痹（帕拉）和无雄性（mle）突变，导致降低表达或功能的α亚单位的电压门控钠通道。与paraandmlemutations一样，Khc突变导致温度敏感性（TS）麻痹。当与异常突变结合时，Khc突变引起合成致死性和TS麻痹的协同增强。此外，Khc突变抑制Shakerandether-a-go-gomatations，破坏钾通道的活动。根据以前的生理测试表明，thakc突变抑制复合动作电位在节段神经传播，这些数据表明，驱动蛋白的活动是需要正常的内向钠电流在神经元动作电位。驱动蛋白和钠/钾ATP酶突变之间的表型相似性和遗传相互作用的测试表明，受损的驱动蛋白功能不影响钠离子的驱动力。我们推测，驱动蛋白功能的丧失抑制了钠通道囊泡的顺行轴突运输。
To investigate the possibility that kinesin transports vesicles bearing proteins essential for ion channel activity, the effects of kinesin (Khc) and ion channel mutations were compared in Drosophila using established tests. Our results show thatKhcmutations produce defects and genetic interactions characteristic ofparalytic(para) andmaleless(mle) mutations that cause reduced expression or function of the alpha-subunit of voltage-gated sodium channels. Likeparaandmlemutations,Khcmutations cause temperature-sensitive (TS) paralysis. When combined withparaormlemutations,Khcmutations cause synthetic lethality and a synergistic enhancement of TS-paralysis. Furthermore,Khcmutations suppressShakerandether-a-go-gomutations that disrupt potassium channel activity. In light of previous physiological tests that show thatKhcmutations inhibit compound action potential propagation in segmental nerves, these data indicate that kinesin activity is required for normal inward sodium currents during neuronal action potentials. Tests for phenotypic similarities and genetic interactions between kinesin and sodium/potassium ATPase mutations suggest that impaired kinesin function does not affect the driving force on sodium ions. We hypothesize that a loss of kinesin function inhibits the anterograde axonal transport of vesicles bearing sodium channels.