Universität zu Köln

Pawlowski, Nikolaus (2010). Dynamin self-assembly and the vesicle scission mechanism How dynamin oligomers cleave the membrane neck of clathrin-coated pits during endocytosis. Bioessays, 32 (12). S. 1033 - 1040. HOBOKEN: WILEY. ISSN 1521-1878

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Abstract

Recently, Gao et al. and Chappie et al. elucidated the crystal structures of the polytetrameric stalk domain of the dynamin-like virus resistance protein, MxA, and of the G-domain dimer of the large, membrane-deforming GTPase, dynamin, respectively. Combined, they provide a hypothetical oligomeric structure for the complete dynamin protein. Here, it is discussed how the oligomers are expected to form and how they participate in dynamin mediated vesicle fission during the process of endocytosis. The proposed oligomeric structure is compared with the novel mechanochemical model of dynamin function recently proposed by Bashkirov et al. and Pucadyil and Schmid. In conclusion, the new model of the dynamin oligomer has the potential to explain how short self-limiting fissogenic dynamin assemblies are formed and how concerted GTP hydrolysis is achieved. The oligomerisation of two other dynamin superfamily proteins, the guanylate binding proteins (GBPs) and the immunity-related GTPases (IRGs), is addressed briefly.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Pawlowski, Nikolaus UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-491143
DOI:	10.1002/bies.201000086
Journal or Publication Title:	Bioessays
Volume:	32
Number:	12
Page Range:	S. 1033 - 1040
Date:	2010
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1521-1878
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language DEPENDENT CONFORMATIONAL-CHANGES; PLECKSTRIN HOMOLOGY DOMAINS; PROLINE-RICH DOMAIN; GTPASE ACTIVITY; NERVE-TERMINALS; ACIDIC PHOSPHOLIPIDS; RESISTANCE GTPASES; SYNAPTIC VESICLES; BULK ENDOCYTOSIS; BINDING PROTEINS Multiple languages Biochemistry & Molecular Biology; Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/49114