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Dyneins

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Dyneins
Nischal K. Karki
William Carey University

BIO 470
Cell Physiology
Dr. Douglas Lipka
Abstract
Dynein is an ATPase from ATP associated with various cell activities family. Cytoplasmic dynein transports various materials from outside the cell to the center body. It is one of the few proteins that can convert the chemical energy of ATP into mechanical. It is a massive macro molecule that is involved with the movement of various organelles within the cell. It is also involved with the movement of a cell in its surrounding, example: movement of spermatozoa using flagella and movement of paramecium using cilia. It has also been identified to be responsible for movement of vital organelles in a cell, for example: movement of organelles in nerve synapses. Thus, any dysfunction of dynein could result in major diseases. Dysfunction of cytoplasmic dynein has been found to be one of the factors of Alzheimer’s disease. Likewise, dysfunction of dynein in flagella has been tracked as one of many causes of infertility in men. It uses microtubule as a track for its movement and heads towards the negative terminal of the microtubule.

Before the 1940’s, actin and myosin based-system was considered responsible for all forms of motility shown by a eukaryotic cell. In 1945, the first account of myosin-like ATPase was recorded by Engelhard. The ATPase was named “spermosin” from bull sperm flagella. After this report many researchers examined the presence of myosin and actin in flagella and cilia. The breakthrough in the field happened during the 1960’s. Gibbons isolated the ATPase protein from Tetrahymena cilia. Since the ATPase displayed properties of isolated sperm flagella and not of myosin, he named the new protein as “dynein” .
Dynein is a part of ATPase associated with diverse cellular activities or AAA family. AAA proteins usually are seen combining as a hexameric rings (six monomers) that carry out specific function as an enzyme. Similarly, dynein also has six



References: Burgess, Stan A., Matt L. Walker, Hitoshi Sakakibara, Peter J. Knight, and Kazuhiro Oiwa. 2003. “Dynein structure and power stroke.” Nature 421: 715-718. doi:10.1038/nature01377. Carter, Andrew P., Carol Cho, Lan Jin, and Ronald D. Vale. 2011. “Crystal Structure of the Dynein Motor Domain.” Science 331: 1159-1165. doi:10.1038/nature01377. Egan, Martin J, Mark A McClintock, and Samara L Reck-Peterson. 2012. “Microtubule-based transport in filamentous fungi.” Current Opinion in Microbiology 15 (6): 637-645. doi:10.1016/j.mib.2012.10.003. Hirokawa, Nobutaka. 1998. “Kinesin and Dynein Superfamily Proteins and the Mechanism of Organelle Transport.” Science 279: 519-526. doi:10.1126/science.279.5350.519. Kanaan, Nicholas M., Gustavo F. Pigino, Scott T. Brady, Orly Lazarov, Lester I. Binder, and Gerardo A. Morfini. 2012. “Axonal degeneration in Alzheimer’s disease: When signaling abnormalities meet the.” Experimental Neurology. doi:10.1016/j.expneurol.2012.06.003. Mohri, Hideo, Kazuo Inabi, Sumio Ishijima, and Shoji A. Baba. 2012. “Tubulin-Dynein System in Flagellar and Ciliary Movement.” Proceedings of the Japan Academy 88 (8): 397-415. doi:10.2183/pjab.88.397. Roberts, Anthony J., Bara Malkova, Matt L. Walker, Hitoshi Sakakibara, Naoki Numata, Takahide Ken, Reiko Ohkura, et al. 2012. “ATP-Driven Remodeling of the Linker Domain.” Structure 1670-1680. Roberts, Anthony J., Naoki Numata, Matt L. Walker, Yusuke S. Kato, Bara Malkova, Takahide Kon, Reiko Ohkura, et al. 2009. “AAA+ Ring and Linker Swing Mechanism in the Dynein Motor.” Cell 136 (3): 485-495. doi:10.1016/j.cell.2008.11.049.

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