dynein
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Function
- cytoplasmic dynein directs minus-end or retrograde transport of vesicles along microtubules, whereas kinesin directs plus-end or anterograde movement
- dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP
- ciliary dynein is the force generating protein of respiratory cilia
- ciliary dynein is required for structural & functional integrity of cilia of ependymal cells lining the brain ventricles
- leading dynein proteins along microtubules shorten their when the load becomes heavy, allowing trailing dyneins to catch up, with the individual proteins bunching together to better share the strain[5]
- aainst even higher loads, dyneins activate catch bonds, attaching themselves to microtubules to ensure they don't get ripped off the track[5]
Structure
- molecules of conventional cytoplasmic dynein are comprised of 2 heavy chain polypeptides & a number of intermediate chains & light chains
- [4] depicts 2 light chains
More general terms
More specific terms
References
- ↑ Stryer Biochemistry WH Freeman & Co, New York, 1988 pg 942
- ↑ Kumar J, Yu H, Sheetz MP. Kinectin, an essential anchor for kinesin-driven vesicle motility. Science. 1995 Mar 24;267(5205):1834-7. PMID: https://www.ncbi.nlm.nih.gov/pubmed/7892610
- ↑ OMIM https://mirror.omim.org/entry/600112
- ↑ 4.0 4.1 Adams JM, Cory S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem Sci. 2001 Jan;26(1):61-6. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/11165519
- ↑ 5.0 5.1 5.2 Rai AK et al Molecular adaptations allow dynein to generate large collective forces inside cells. Cell, 152:172-82, 2013 PMID: https://www.ncbi.nlm.nih.gov/pubmed/23332753