The dynamin-cortactin complex as a mediator of vesicle formation at the trans-Golgi network

Shaun Weller, Hong Cao, Mark A. McNiven

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The conventional dynamins represent a family of large GTPases that are encoded by at leastthree distinct genes in mammalian tissue and contain four conserved domains; an N-terminal highly conserved tripartite GTP-binding domain located within the first 300 amino acids, a pleckstrin homology (PH) domain of 100 amino acids, a coiled-coil (CC) region and a modestly conserved proline-rich domain (PRD) at the C terminus. Several in vitro and in vivo studies have demonstrated convincingly that dynamin binds to phosphoinositides via its PH domain (Salim et al. 1996; Zheng et al. 1996; Achiriloaie et al. 1999; Lee et al. 1999; Vallis et al. 1999), facilitating a direct interaction of dynamin with membranes. The CC domain has been characterized as a GTPase-effector domain (GED) (Sever et al. 1999), whereas the PRD has been shown to bind to multiple effector molecules (for a review of these see (2000a).

Original languageEnglish (US)
Title of host publicationThe Golgi Apparatus
Subtitle of host publicationState of the Art 110 Years after Camillo Golgi's Discovery
PublisherSpringer Verlag
Pages301-313
Number of pages13
ISBN (Electronic)9783211763100
ISBN (Print)9783211763094
DOIs
StatePublished - Jan 1 2008

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Weller, S., Cao, H., & McNiven, M. A. (2008). The dynamin-cortactin complex as a mediator of vesicle formation at the trans-Golgi network. In The Golgi Apparatus: State of the Art 110 Years after Camillo Golgi's Discovery (pp. 301-313). Springer Verlag. https://doi.org/10.1007/978-3-211-76310-0_18