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

Santosh Kumar, Y. Zhou, M. Plamann

Research output: Contribution to journalArticle

23 Citations (Scopus)

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. 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.

Original languageEnglish (US)
Pages (from-to)939-944
Number of pages6
JournalEMBO Reports
Volume2
Issue number10
DOIs
StatePublished - Nov 20 2001

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Membranes
Dyneins
Cytoplasmic Dyneins
Dynactin Complex
Fungi
Neurospora crassa
Microtubules
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Dynactin-membrane interaction is regulated by the C-terminal domains of p150Glued . / Kumar, Santosh; Zhou, Y.; Plamann, M.

In: EMBO Reports, Vol. 2, No. 10, 20.11.2001, p. 939-944.

Research output: Contribution to journalArticle

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