摘要
细胞膜系统的动态变化是原核与真核细胞中多种细胞功能实现的基础。在真核细胞中,膜的融合与分裂过程是由动力蛋白(dynamin)家族的GTP酶催化的,然而,这一机制在原核生物中却少有研究。文章总结了现有原核生物动力蛋白最新的结构和生化数据结果,探讨了它们的结构及功能特性。通过分析动力蛋白家族及其蛋白质功能域在原核生物中的进化分布,初步揭示了该蛋白家族的进化历史和功能演化,并且进一步探讨了动力蛋白参与脂滴形成和分裂过程的可能机制。基于以上研究,最后给出了动力蛋白参与脂滴动态变化的假说模型,以便于原核生物动力蛋白的功能研究。
Membrane dynamics are essential for the numerous cellular processes in eukaryotic and prokaryotic cells. Membrane fusion and fission are often catalysed by large GTPases of the dynamin protein families in eukaryotic cells, however the mechanisms responsible in prokaryotes are yet to be investigated in depth. With new results of the structural and biochemical data of prokaryotic dynamin-like proteins(DLPs) becoming available, this review summarizes current knowledge regarding prokaryotic dynamins, and discusses their structural and functional properties. The mechanisms how DLPs are involved in lipid droplets(LDs) formation and fission are investigated, and highlighted as a potential research area of LD dynamics. Based on these understandings, a hypothetical model is then described and further research analysis proposed.
出处
《生物物理学报》
CAS
CSCD
北大核心
2013年第9期646-657,共12页
Acta Biophysica Sinica
基金
国家自然科学基金项目(61273228,61103073)
天津市科委自然科学基金项目(11JCYBJC26600)~~
关键词
动力蛋白
脂滴
功能进化
蛋白质功能域
膜动力学
Dynamin-like protein
Lipid droplet
Functional evolution
Protein domain
Membrane dynamics