Apoptotic Cleavage of Cytoplasmic Dynein Intermediate Chain and p150GluedStops Dynein-Dependent Membrane Motility

Cytoplasmic dynein is the major minus endirected microtubule motor in animal cells, and associates with many of its cargoes in conjunction with the dynactin complex. Interaction between cytoplasmic dynein and dynactin is mediated by the binding of cytoplasmic dynein intermediate chains (CD-IC) to th...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of cell biology Vol. 153; no. 7; pp. 1415 - 1426
Main Authors Lane, Jon D., Maïlys A. S. Vergnolle, Woodman, Philip G., Allan, Victoria J.
Format Journal Article
LanguageEnglish
Published Rockefeller University Press 25.06.2001
The Rockefeller University Press
Subjects
Antibodies
Apoptosis
Cell cycle
Cytosol
Eggs
Freight
Immunoblotting
Microtubules
Molecules
Original
P branes
Online AccessGet full text

Cover

More Information
Summary:Cytoplasmic dynein is the major minus endirected microtubule motor in animal cells, and associates with many of its cargoes in conjunction with the dynactin complex. Interaction between cytoplasmic dynein and dynactin is mediated by the binding of cytoplasmic dynein intermediate chains (CD-IC) to the dynactin subunit, p150Glued. We have found that both CD-IC and p150Gluedare cleaved by caspases during apoptosis in cultured mammalian cells and in Xenopus egg extracts. Xenopus CD-IC is rapidly cleaved at a conserved aspartic acid residue adjacent to its NH2-terminal p150Gluedbinding domain, resulting in loss of the otherwise intact cytoplasmic dynein complex from membranes. Cleavage of CD-IC and p150Gluedin apoptotic Xenopus egg extracts causes the cessation of cytoplasmic dynein-driven endoplasmic reticulum movement. Motility of apoptotic membranes is restored by recruitment of intact cytoplasmic dynein and dynactin from control cytosol, or from apoptotic cytosol supplemented with purified cytoplasmic dynein-dynactin, demonstrating the dynamic nature of the association of cytoplasmic dynein and dynactin with their membrane cargo.
ISSN:0021-9525
1540-8140