Academic Journal

Dynamin-catalyzed membrane fission requires coordinated GTP hydrolysis.

التفاصيل البيبلوغرافية
العنوان: Dynamin-catalyzed membrane fission requires coordinated GTP hydrolysis.
المؤلفون: Ya-Wen Liu, Juha-Pekka Mattila, Sandra L Schmid
المصدر: PLoS ONE, Vol 8, Iss 1, p e55691 (2013)
بيانات النشر: Public Library of Science (PLoS), 2013.
سنة النشر: 2013
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Dynamin is the most-studied membrane fission machinery and has served as a paradigm for studies of other fission GTPases; however, several critical questions regarding its function remain unresolved. In particular, because most dynamin GTPase domain mutants studied to date equally impair both basal and assembly-stimulated GTPase activities, it has been difficult to distinguish their respective roles in clathrin-mediated endocytosis (CME) or in dynamin catalyzed membrane fission. Here we compared a new dynamin mutant, Q40E, which is selectively impaired in assembly-stimulated GTPase activity with S45N, a GTP-binding mutant equally defective in both basal and assembly-stimulated GTPase activities. Both mutants potently inhibit CME and effectively recruit other endocytic accessory proteins to stalled coated pits. However, the Q40E mutant blocks at a later step than S45N, providing additional evidence that GTP binding and/or basal GTPase activities of dynamin are required throughout clathrin coated pit maturation. Importantly, using in vitro assays for assembly-stimulated GTPase activity and membrane fission, we find that the latter is much more potently inhibited by both dominant-negative mutants than the former. These studies establish that efficient fission from supported bilayers with excess membrane reservoir (SUPER) templates requires coordinated GTP hydrolysis across two rungs of an assembled dynamin collar.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC3561337?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0055691
URL الوصول: https://doaj.org/article/cd4b83cbc90d4ff1a7eca72e7139c43e
رقم الانضمام: edsdoj.4b83cbc90d4ff1a7eca72e7139c43e
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0055691