Dynactin–membrane interaction is regulated by the C-terminal domains of p150Glued

AUTOR(ES)

Kumar, Santosh

FONTE

Oxford University Press

RESUMO

Dynactin has been proposed to link the microtubule-associated motor cytoplasmic dynein with membranous cargo; however, the mechanism by which dynactin–membrane interaction is regulated is unknown. Here we show that dynein and dynactin exist in discrete cytosolic and membrane-bound states in the filamentous fungus Neurospora crassa. Results from in vitro membrane-binding studies show that dynein and dynactin–membrane interaction is co-dependent. p150Glued of dynactin has been shown to interact with dynein intermediate chain and dynactin Arp1 filament; however, it is not known to play a direct role in membrane binding. In this report we describe our analysis of 43 p150Glued mutants, and we show that C-terminal deletions which remove the terminal coiled-coil (CC2) and basic domain (BD) result in constitutive dynactin–membrane binding. In vitro addition of recombinant p150Glued CC2+BD protein blocks dynactin–membrane binding. We propose that the C-terminal domains of p150Glued regulate dynactin–membrane binding through a steric mechanism that controls accessibility of the Arp1 filament of dynactin to membranous cargo.

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