Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington, United States; School of Medical Sciences, University of New South Wales, Sydney, New South Wales, Australia.
Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, Washington, United States.
Mol Cell Neurosci. 2017 Oct;84:48-57. doi: 10.1016/j.mcn.2017.04.002. Epub 2017 Apr 19.
Actin is a profoundly influential protein; it impacts, among other processes, membrane morphology, cellular motility, and vesicle transport. Actin can polymerize into long filaments that push on membranes and provide support for intracellular transport. Actin filaments have polar ends: the fast-growing (barbed) end and the slow-growing (pointed) end. Depolymerization from the pointed end supplies monomers for further polymerization at the barbed end. Tropomodulins (Tmods) cap pointed ends by binding onto actin and tropomyosins (Tpms). Tmods and Tpms have been shown to regulate many cellular processes; however, very few studies have investigated their joint role in the nervous system. Recent data directly indicate that they can modulate neuronal morphology. Additional studies suggest that Tmod and Tpm impact molecular processes influential in synaptic signaling. To facilitate future research regarding their joint role in actin regulation in the nervous system, we will comprehensively discuss Tpm and Tmod and their known functions within molecular systems that influence neuronal development.
肌动蛋白是一种极具影响力的蛋白质；它影响着膜形态、细胞运动和囊泡运输等过程。肌动蛋白可以聚合成长丝，推动膜并为细胞内运输提供支持。肌动蛋白丝有极性末端：快速生长（有棘）的末端和缓慢生长（尖）的末端。从尖的末端解聚提供单体，以供在有棘的末端进一步聚合。肌动蛋白末端帽（Tmods）通过与肌动蛋白和原肌球蛋白（Tpms）结合来封闭尖的末端。Tmods 和 Tpms 已被证明可以调节许多细胞过程；然而，很少有研究调查它们在神经系统中的联合作用。最近的数据直接表明，它们可以调节神经元形态。其他研究表明，Tmod 和 Tpm 影响突触信号传递中具有影响力的分子过程。为了促进未来关于它们在神经系统中调节肌动蛋白的联合作用的研究，我们将全面讨论 Tpm 和 Tmod 及其在影响神经元发育的分子系统中的已知功能。
