ArticleThe Journal of cell biology1994
Cytoplasmic dynein undergoes intracellular redistribution concomitant with phosphorylation of the heavy chain in response to serum starvation and okadaic acid.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 87 citations in OpenAlex.
- Distinct functional roles of cytoplasmic dynein defined by the intermediate chain isoforms.Experimental cell research · 2015Review
- Interaction of SQSTM1 with the motor protein dynein--SQSTM1 is required for normal dynein function and trafficking.Journal of cell science · 2014Article
- Live cell imaging reveals differential modifications to cytoplasmic dynein properties by phospho- and dephosphomimic mutations of the intermediate chain 2C S84.Journal of neuroscience research · 2014Article
- Recycling of kinesin-1 motors by diffusion after transport.PloS one · 2013Article
- Mitochondrial metabolism in Parkinson's disease impairs quality control autophagy by hampering microtubule-dependent traffic.Human molecular genetics · 2012Article
- Trk activation of the ERK1/2 kinase pathway stimulates intermediate chain phosphorylation and recruits cytoplasmic dynein to signaling endosomes for retrograde axonal transport.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Dynein dysfunction induces endocytic pathology accompanied by an increase in Rab GTPases: a potential mechanism underlying age-dependent endocytic dysfunction.The Journal of biological chemistry · 2009Article
- SPD-3 is required for spindle alignment in Caenorhabditis elegans embryos and localizes to mitochondria.Genetics · 2007Article
- Nuclear localization signal peptides induce molecular delivery along microtubules.Biophysical journal · 2005Article
- Role of KIFC3 motor protein in Golgi positioning and integration.The Journal of cell biology · 2002Article
- Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport.The Journal of cell biology · 2001Article
- Apoptotic cleavage of cytoplasmic dynein intermediate chain and p150(Glued) stops dynein-dependent membrane motility.The Journal of cell biology · 2001Article
- Dynein, dynactin, and kinesin II's interaction with microtubules is regulated during bidirectional organelle transport.The Journal of cell biology · 2000Article
- Increased protein phosphorylation of cytoplasmic dynein results in impaired motor function.The Biochemical journal · 1999Article
- Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Characterization of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells.The Journal of cell biology · 1998Article
- Article
- Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution.The Journal of cell biology · 1997Article
- Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18.Molecular and cellular biology · 1997Article
- Molecular requirements for bi-directional movement of phagosomes along microtubules.The Journal of cell biology · 1997Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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