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PMID: 11018061 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Retracted Publication

Dynein, dynactin, and kinesin II's interaction with microtubules is regulated during bidirectional organelle transport.

The Journal of cell biology ·Vol. 151 ·No. 1 ·2000-10-02 ·Pages 155-66

Reese EL, Haimo LT

Abstract

The microtubule motors, cytoplasmic dynein and kinesin II, drive pigmented organelles in opposite directions in Xenopus melanophores, but the mechanism by which these or other motors are regulated to control the direction of organelle transport has not been previously elucidated. We find that cytoplasmic dynein, dynactin, and kinesin II remain on pigment granules during aggregation and dispersion in melanophores, indicating that control of direction is not mediated by a cyclic association of motors with these organelles. However, the ability of dynein, dynactin, and kinesin II to bind to microtubules varies as a function of the state of aggregation or dispersion of the pigment in the cells from which these molecules are isolated. Dynein and dynactin bind to microtubules when obtained from cells with aggregated pigment, whereas kinesin II binds to microtubules when obtained from cells with dispersed pigment. Moreover, the microtubule binding activity of these motors/dynactin can be reversed in vitro by the kinases and phosphatase that regulate the direction of pigment granule transport in vivo. These findings suggest that phosphorylation controls the direction of pigment granule transport by altering the ability of dynein, dynactin, and kinesin II to interact with microtubules.

MeSH Terms
Animals Biological Transport Calcium-Binding Proteins/metabolism Cell Line Cyclic AMP-Dependent Protein Kinases/metabolism Cytoplasmic Granules/metabolism Dynactin Complex Dyneins/metabolism Kinesins Melanophores Microtubule-Associated Proteins/metabolism Microtubules/metabolism Models, Biological Molecular Motor Proteins/physiology Movement/physiology Muscle Proteins/metabolism Organelles/physiology Phosphoprotein Phosphatases/metabolism Pigments, Biological/metabolism Protein Binding Protein Kinase C/metabolism Solubility Xenopus Xenopus Proteins
Chemicals
Calcium-Binding Proteins Dynactin Complex Microtubule-Associated Proteins Molecular Motor Proteins Muscle Proteins Pigments, Biological XKLP3 protein, Xenopus Xenopus Proteins kinesin-II Cyclic AMP-Dependent Protein Kinases Protein Kinase C Phosphoprotein Phosphatases Dyneins Kinesins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Reese E L
Department of Biology, University of California at Riverside, Riverside, California 92521, USA.
Haimo L T
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.151.1.155
Published
2000-10-02
Pages
155-66
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2189799
Subset
IM
Corrections
RetractionIn
PMID: 12569089
External Links
PubMed source DOI: 10.1083/jcb.151.1.155 PMC Full Text View journal details
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