缢断蛋白
缢断蛋白(英語:Dynamin,也译为发动蛋白、动力蛋白)是一种与真核生物內吞作用有关的GTP酶(GTPase),参与网格蛋白介导的内吞作用(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 | |||||||||
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鑑定 | |||||||||
標誌 | Dynamin_N | ||||||||
Pfam | PF00350(旧版) | ||||||||
Pfam宗系 | CL0023(旧版) | ||||||||
InterPro | IPR001401 | ||||||||
PROSITE | PDOC00362 | ||||||||
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Dynamin central region | |||||||||
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![]() Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus | |||||||||
鑑定 | |||||||||
標誌 | Dynamin_M | ||||||||
Pfam | PF01031(旧版) | ||||||||
InterPro | IPR000375 | ||||||||
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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-末端的富脯氨酸结构域(用于结合SH3结构域的蛋白)[5]。
類型
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
- ^ 1.0 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.