Journal article
Dynamin Interacts with Members of the Sumoylation Machinery*
Abstract
Dynamin is a GTP-binding protein whose oligomerization-dependent assembly around the necks of lipid vesicles mediates their scission from parent membranes. Dynamin is thus directly involved in the regulation of endocytosis. Sumoylation is a post-translational protein modification whereby the ubiquitin-like modifier Sumo is covalently attached to lysine residues on target proteins by a process requiring the concerted action of an activating …
Authors
Mishra RK; Jatiani SS; Kumar A; Simhadri VR; Hosur RV; Mittal R
Journal
Journal of Biological Chemistry, Vol. 279, No. 30, pp. 31445–31454
Publisher
Elsevier
Publication Date
July 2004
DOI
10.1074/jbc.m402911200
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AnimalsBase SequenceBinding SitesCHO CellsCarrier ProteinsCricetinaeDNA PrimersDynamin IHumansIn Vitro TechniquesKineticsModels, MolecularProtein Inhibitors of Activated STATProtein Structure, TertiaryRecombinant ProteinsSUMO-1 ProteinSmall Ubiquitin-Related Modifier ProteinsTwo-Hybrid System TechniquesUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9