Abstract:
: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. p150(Glued) 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 p150(Glued) 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 p150(Glued) CC2+BD protein blocks dynactin-membrane binding. We propose that the C-terminal domains of p150(Glued) regulate dynactin-membrane binding through a steric mechanism that controls accessibility of the Arp1 filament of dynactin to membranous cargo.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Kumar S,Zhou Y,Plamann Mdoi
10.1093/embo-reports/kve202keywords:
subject
Has Abstractpub_date
2001-10-01 00:00:00pages
939-44issue
10eissn
1469-221Xissn
1469-3178pii
kve202journal_volume
2pub_type
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