Structural Insights into Dynamin-Mediated Membrane Fission

被引：50

作者：

Faelber, Katja ^{[1
]}

Held, Martin ^{[2
]}

Gao, Song ^{[1
,4
]}

Posor, York ^{[3
]}

Haucke, Volker ^{[3
]}

Noe, Frank ^{[2
]}

Daumke, Oliver ^{[1
,5
]}

机构：

[1] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany

[2] Free Univ Berlin, Inst Math, D-14195 Berlin, Germany

[3] Free Univ Berlin, Inst Chem & Biochem, D-14195 Berlin, Germany

[4] Sun Yat Sen Univ, State Key Lab Oncol S China, Ctr Canc, Guangzhou 510060, Guangdong, Peoples R China

[5] Charite, Inst Med Phys & Biophys, D-10117 Berlin, Germany

来源：

STRUCTURE | 2012年 / 20卷 / 10期

关键词：

DEPENDENT CONFORMATIONAL-CHANGES; PLECKSTRIN HOMOLOGY DOMAINS; CRYSTAL-STRUCTURE; GTPASE ACTIVITY; ACIDIC PHOSPHOLIPIDS; NUCLEOTIDE-FREE; BAR DOMAINS; PH DOMAIN; ENDOCYTOSIS; PROTEIN;

D O I：

10.1016/j.str.2012.08.028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Dynamin is a multidomain mechanochemical guanine triphosphatase that catalyzes membrane scission, most notably of clathrin-coated endocytic vesicles. A number of recent publications have provided structural and mechanistic insights into the formation of helical dynamin filaments assembled by dynamic interactions of multiple domains within dynamin. As a prerequisite for membrane scission, this oligomer undergoes nucleotide-triggered large scale dynamic rearrangements. Here, we review these structural findings and discuss how the architecture of dynamin is poised for the assembly into right-handed helical filaments. Based on these data, we propose a structure-based model for dynamin-mediated scission of membranes.

引用

收藏

页码：1621 / 1628

页数：8

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