کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2039760 1073080 2014 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A Dynamin Mutant Defines a Superconstricted Prefission State
ترجمه فارسی عنوان
یک جهش دینامین یک دولت پیش فشرده فوق ستاره ای را تعریف می کند
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک علوم کشاورزی و بیولوژیک (عمومی)
چکیده انگلیسی


• Cryo-EM data show a superconstricted dynamin polymer that reaches the fission limit
• Dynamin superconstriction occurs without GTP hydrolysis
• Two-start symmetry yields preferred packing of dynamin subunits on a membrane surface
• PRD interaction domain localizes to the exterior of the superconstricted dynamin tube

SummaryDynamin is a 100 kDa GTPase that organizes into helical assemblies at the base of nascent clathrin-coated vesicles. Formation of these oligomers stimulates the intrinsic GTPase activity of dynamin, which is necessary for efficient membrane fission during endocytosis. Recent evidence suggests that the transition state of dynamin’s GTP hydrolysis reaction serves as a key determinant of productive fission. Here, we present the structure of a transition-state-defective dynamin mutant K44A trapped in a prefission state at 12.5 Å resolution. This structure constricts to 3.7 nm, reaching the theoretical limit required for spontaneous membrane fission. Computational docking indicates that the ground-state conformation of the dynamin polymer is sufficient to achieve this superconstricted prefission state and reveals how a two-start helical symmetry promotes the most efficient packing of dynamin tetramers around the membrane neck. These data suggest a model for the assembly and regulation of the minimal dynamin fission machine.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 8, Issue 3, 7 August 2014, Pages 734–742
نویسندگان
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