The crystal structure of dynamin

被引：206

作者：

Ford, Marijn G. J. ^{[1
]}

Jenni, Simon ^{[2
]}

Nunnari, Jodi ^{[1
]}

机构：

[1] Univ Calif Davis, Dept Mol & Cellular Biol, Davis, CA 95616 USA

[2] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

NATURE | 2011年 / 477卷 / 7366期

关键词：

PLECKSTRIN HOMOLOGY DOMAIN; CLATHRIN-MEDIATED ENDOCYTOSIS; GTPASE ACTIVITY; IN-VIVO; CONFORMATIONAL-CHANGES; BINDING PROTEINS; MECHANISM; FISSION; MITOCHONDRIAL; CONSTRICTION;

D O I：

10.1038/nature10441

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Dynamin-related proteins (DRPs) are multi-domain GTPases that function via oligomerization and GTP-dependent conformational changes to play central roles in regulating membrane structure across phylogenetic kingdoms. How DRPs harness self-assembly and GTP-dependent conformational changes to remodel membranes is not understood. Here we present the crystal structure of an assembly-deficient mammalian endocytic DRP, dynamin 1, lacking the proline-rich domain, in its nucleotide-free state. The dynamin 1 monomer is an extended structure with the GTPase domain and bundle signalling element positioned on top of a long helical stalk with the pleckstrin homology domain flexibly attached on its opposing end. Dynamin 1 dimer and higher order dimer multimers form via interfaces located in the stalk. Analysis of these interfaces provides insight into DRP family member specificity and regulation and provides a framework for understanding the biogenesis of higher order DRP structures and the mechanism of DRP-mediated membrane scission events.

引用

页码：561 / 566

页数：6

共 42 条

[1]

Achiriloaie M, 1999, MOL CELL BIOL, V19, P1410

[2] The Proline/Arginine-Rich Domain Is a Major Determinant of Dynamin Self-Activation [J].

Barylko, Barbara ;

Wang, Lei ;

Binns, Derk D. ;

Ross, Justin A. ;

Tassin, Tara C. ;

Collins, Katie A. ;

Jameson, David M. ;

Albanesi, Joseph P. .

BIOCHEMISTRY, 2010, 49 (50) :10592-10594

[3] GTPase Cycle of Dynamin Is Coupled to Membrane Squeeze and Release, Leading to Spontaneous Fission [J].

Bashkirov, Pavel V. ;

Akimov, Sergey A. ;

Evseev, Alexey I. ;

Schmid, Sandra L. ;

Zimmerberg, Joshua ;

Frolov, Vadim A. .

CELL, 2008, 135 (07) :1276-1286

[4] Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes [J].

Bian, Xin ;

Klemm, Robin W. ;

Liu, Tina Y. ;

Zhang, Miao ;

Sun, Sha ;

Sui, Xuewu ;

Liu, Xinqi ;

Rapoport, Tom A. ;

Hu, Junjie .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (10) :3976-3981

[5] Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A [J].

Byrnes, Laura J. ;

Sondermann, Holger .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (06) :2216-2221

[6] G domain dimerization controls dynamin's assembly-stimulated GTPase activity [J].

Chappie, Joshua S. ;

Acharya, Sharmistha ;

Leonard, Marilyn ;

Schmid, Sandra L. ;

Dyda, Fred .

NATURE, 2010, 465 (7297) :435-U54

[7] An Intramolecular Signaling Element that Modulates Dynamin Function In Vitro and In Vivo [J].

Chappie, Joshua S. ;

Acharya, Sharmistha ;

Liu, Ya-Wen ;

Leonard, Marilyn ;

Pucadyil, Thomas J. ;

Schmid, Sandra L. .

MOLECULAR BIOLOGY OF THE CELL, 2009, 20 (15) :3561-3571

[8] Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin [J].

Danino, D ;

Moon, KH ;

Hinshaw, JE .

JOURNAL OF STRUCTURAL BIOLOGY, 2004, 147 (03) :259-267

[9] Dynamin 2 and human diseases [J].

Durieux, Anne-Cecile ;

Prudhon, Bernard ;

Guicheney, Pascale ;

Bitoun, Marc .

JOURNAL OF MOLECULAR MEDICINE-JMM, 2010, 88 (04) :339-350

[10] CRYSTAL-STRUCTURE AT 2.2-ANGSTROM RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN [J].

FERGUSON, KM ;

LEMMON, MA ;

SCHLESSINGER, J ;

SIGLER, PB .

CELL, 1994, 79 (02) :199-209

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