In April 2016 Manchester eScholar was replaced by the University of Manchester’s new Research Information Management System, Pure. In the autumn the University’s research outputs will be available to search and browse via a new Research Portal. Until then the University’s full publication record can be accessed via a temporary portal and the old eScholar content is available to search and browse via this archive.

Related resources

Full-text held externally

University researcher(s)

Academic department(s)

Roles of dynein and dynactin in early endosome dynamics revealed using automated tracking and global analysis.

Flores-Rodriguez, Neftali; Rogers, Salman S; Kenwright, David A; Waigh, Thomas A; Woodman, Philip G; Allan, Victoria J

PloS one. 2011;6(9):e24479.

Access to files

Full-text and supplementary files are not available from Manchester eScholar. Full-text is available externally using the following links:

Full-text held externally

Abstract

Microtubule-dependent movement is crucial for the spatial organization of endosomes in most eukaryotes, but as yet there has been no systematic analysis of how a particular microtubule motor contributes to early endosome dynamics. Here we tracked early endosomes labeled with GFP-Rab5 on the nanometer scale, and combined this with global, first passage probability (FPP) analysis to provide an unbiased description of how the minus-end microtubule motor, cytoplasmic dynein, supports endosome motility. Dynein contributes to short-range endosome movement, but in particular drives 85-98% of long, inward translocations. For these, it requires an intact dynactin complex to allow membrane-bound p150(Glued) to activate dynein, since p50 over-expression, which disrupts the dynactin complex, inhibits inward movement even though dynein and p150(Glued) remain membrane-bound. Long dynein-dependent movements occur via bursts at up to ∼8 µms(-1) that are linked by changes in rate or pauses. These peak speeds during rapid inward endosome movement are still seen when cellular dynein levels are 50-fold reduced by RNAi knock-down of dynein heavy chain, while the number of movements is reduced 5-fold. Altogether, these findings identify how dynein helps define the dynamics of early endosomes.

Bibliographic metadata

Type of resource:
Content type:
Publication type:
Published date:
Journal title:
Abbreviated journal title:
ISSN:
Place of publication:
United States
Volume:
6
Issue:
9
Pagination:
e24479
Digital Object Identifier:
10.1371/journal.pone.0024479
Pubmed Identifier:
21915335
Pii Identifier:
PONE-D-11-09871
Access state:
Active

Institutional metadata

University researcher(s):
Academic department(s):

Record metadata

Manchester eScholar ID:
uk-ac-man-scw:136823
Created by:
Woodman, Philip
Created:
17th November, 2011, 13:17:48
Last modified by:
Woodman, Philip
Last modified:
26th October, 2015, 14:36:25

Can we help?

The library chat service will be available from 11am-3pm Monday to Friday (excluding Bank Holidays). You can also email your enquiry to us.