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

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).