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Dynactin–membrane interaction is regulated by the C‐terminal domains of p150 Glued
Author(s) -
Kumar Santosh,
Zhou Yi,
Plamann Michael
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve202
Subject(s) - dynactin , dynein , microbiology and biotechnology , microtubule , biophysics , cytoplasm , biology , chemistry
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.