缢断蛋白

缢断蛋白(英语:Dynamin,也译为发动蛋白动力蛋白)是一种与真核生物内吞作用有关的GTP酶英语GTPase(GTPase),参与网格蛋白介导的内吞作用英语Receptor-mediated endocytosis(clathrin-mediated endocytosis,CME)等各种膜裂变和融合过程。在CME的最后阶段,缢断蛋白组装并充当机械化学支架,使内陷的网格蛋白包被小窝(clathrin-coated pit,CCP)颈部的膜收缩和变形,并从细胞膜上切下新生囊泡[1][2]

缢断蛋白
融合了盘基网柄菌Dictyostelium discoideum)的无核苷酸肌球蛋白II运动结构域和大鼠Rattus norvegicus)的缢断蛋白I GTPase结构域的结构。
鉴定
标志Dynamin_N
PfamPF00350旧版
Pfam宗系CL0023旧版
InterPro英语InterProIPR001401
PROSITE英语PROSITEPDOC00362
Dynamin central region
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
鉴定
标志Dynamin_M
PfamPF01031旧版
InterPro英语InterProIPR000375

缢断蛋白与其类似的蛋白属于一个“缢断蛋白超家族”(dynamin superfamily,DSP),成员包括:MX1(干扰素诱导的GTP结合蛋白1)、MFN1(线粒体融合蛋白1)、GBPs(鸟苷酸结合蛋白)等,都与细胞膜融合有关[3][4]

结构

缢断蛋白大小约96 kDa,长约900个氨基酸残基,从N-末端开始依次为GTP酶结构域(用于结合GTP)、富α螺旋区域、PH结构域(用于结合脂质)到C-末端富脯氨酸结构域(用于结合SH3结构域的蛋白)[5]

类型

在哺乳动物中,有三种不同的缢断蛋白基因,三者的PH结构域关键序列存在差异:

参考文献

  1. ^ 1.0 1.1 Henley JR, Cao H, McNiven MA. Participation of dynamin in the biogenesis of cytoplasmic vesicles. FASEB Journal. December 1999,. 13 Suppl 2 (9002): S243–7. PMID 10619136. doi:10.1096/fasebj.13.9002.S243. 
  2. ^ Cheng, Xiaodong; Chen, Kuangcai; Dong, Bin; Yang, Meek; Filbrun, Seth L.; Myoung, Yong; Huang, Teng-Xiang; Gu, Yan; Wang, Gufeng; Fang, Ning. Dynamin-dependent vesicle twist at the final stage of clathrin-mediated endocytosis. Nature Cell Biology. 2021-07-12. doi:10.1038/s41556-021-00713-x. 
  3. ^ Hinshaw, J. "Research statement, Jenny E. Hinshaw, Ph.D."页面存档备份,存于互联网档案馆) National Institute of Diabetes & Digestive & Kidney Diseases, Laboratory of Cell Biochemistry and Biology. Accessed 19 March 2013.
  4. ^ Urrutia R, Henley JR, Cook T, McNiven MA. The dynamins: redundant or distinct functions for an expanding family of related GTPases?. Proceedings of the National Academy of Sciences of the United States of America. January 1997, 94 (2): 377–84. PMC 34135 . PMID 9012790. doi:10.1073/pnas.94.2.377. 
  5. ^ Jimah, JR; Hinshaw, JE. Structural Insights into the Mechanism of Dynamin Superfamily Proteins.. Trends in cell biology. 2019-03, 29 (3): 257–273. PMID 30527453. doi:10.1016/j.tcb.2018.11.003. 
  6. ^ Praefcke GJ, McMahon HT. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nature Reviews. Molecular Cell Biology. February 2004, 5 (2): 133–147. PMID 15040446. S2CID 6305282. doi:10.1038/nrm1313. 

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