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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Collins, C. A. Lin, S. X. Ferro, K. L. |
| Description | Author Affiliation: Lin SX ( Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611-3008.) |
| Abstract | Cytoplasmic dynein is a microtubule-binding protein which is considered to serve as a motor for retrograde organelle movement. In cultured fibroblasts, cytoplasmic dynein localizes primarily to lysosomes, membranous organelles whose movement and distribution in the cytoplasm have been shown to be dependent on the integrity of the microtubule cytoskeleton. We have recently identified conditions which lead to an apparent dissociation of dynein from lysosomes in vivo, indicating that alterations in membrane binding may be involved in the regulation of retrograde organelle movement (Lin, S. X. H., and C. A. Collins. 1993. J. Cell Sci. 105:579-588). Both brief serum withdrawal and low extracellular calcium levels induced this alteration, and the effect was reversed upon addition of serum or additional calcium. Here we demonstrate that the phosphorylation state of the dynein molecule is correlated with changes in its intracellular distribution in normal rat kidney fibroblasts. Dynein heavy chain phosphorylation level increased during serum starvation, and decreased back to control levels upon subsequent addition of serum. We found that okadaic acid, a phosphoprotein phosphatase inhibitor, mimicked the effects of serum starvation on both phosphorylation and the intracellular redistribution of dynein from a membrane-associated pool to one that was more soluble, with similar dose dependence for both phenomena. Cell fractionation by differential detergent extraction revealed that a higher proportion of dynein was present in a soluble pool after serum starvation than was found in comparable fractions from control cells. Our data indicate that cytoplasmic dynein is phosphorylated in vivo, and changes in phosphorylation state may be involved in a regulatory mechanism affecting the distribution of this protein among intracellular compartments. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 4 |
| Volume Number | 127 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1994-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Dyneins Metabolism Ethers, Cyclic Pharmacology 8-Bromo Cyclic Adenosine Monophosphate Adenosine Triphosphate Alkaloids Animals Bucladesine Calcimycin Calmodulin Antagonists & Inhibitors Cell Line Colforsin Culture Media Cytoplasm Edetic Acid Imidazoles Kidney Kinetics Macromolecular Substances Okadaic Acid Phosphates Phosphoprotein Phosphatases Phosphorus Radioisotopes Phosphorylation Staurosporine Sulfonamides Tetradecanoylphorbol Acetate Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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