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Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement.
In cell biology, the spindle apparatus is the cytoskeletal structure of eukaryotic cells that forms during cell division to separate sister chromatids between daughter cells. It is referred to as the mitotic spindle during mitosis, a process that produces genetically identical daughter cells, or the meiotic spindle during meiosis, a process that produces gametes with half the number of chromosomes of the parent cell.
Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton. It was discovered and named by Hideo Mōri in 1968. Microtubules function in many essential cellular processes, including mitosis. Tubulin-binding drugs kill cancerous cells by inhibiting microtubule dynamics, which are required for DNA segregation and therefore cell division.
Timothy John Mitchison is a cell biologist and systems biologist and Hasib Sabbagh Professor of Systems Biology at Harvard Medical School in the United States. He is known for his discovery, with Marc Kirschner, of dynamic instability in microtubules, for studies of the mechanism of cell division, and for contributions to chemical biology.
Katanin is a microtubule-severing AAA protein. It is named after the Japanese sword called a katana. Katanin is a heterodimeric protein first discovered in sea urchins. It contains a 60 kDa ATPase subunit, encoded by KATNA1, which functions to sever microtubules. This subunit requires ATP and the presence of microtubules for activation. The second 80 kDA subunit, encoded by KATNB1, regulates the activity of the ATPase and localizes the protein to centrosomes. Electron microscopy shows that katanin forms 14–16 nm rings in its active oligomerized state on the walls of microtubules.
In molecular biology, treadmilling is a phenomenon observed within protein filaments of the cytoskeletons of many cells, especially in actin filaments and microtubules. It occurs when one end of a filament grows in length while the other end shrinks, resulting in a section of filament seemingly "moving" across a stratum or the cytosol. This is due to the constant removal of the protein subunits from these filaments at one end of the filament, while protein subunits are constantly added at the other end. Treadmilling was discovered by Wegner, who defined the thermodynamic and kinetic constraints. Wegner recognized that: “The equilibrium constant (K) for association of a monomer with a polymer is the same at both ends, since the addition of a monomer to each end leads to the same polymer.”; a simple reversible polymer can’t treadmill; ATP hydrolysis is required. GTP is hydrolyzed for microtubule treadmilling.
Eva Nogales is a Spanish-American biophysicist at the Lawrence Berkeley National Laboratory and a professor at the University of California, Berkeley, where she served as head of the Division of Biochemistry, Biophysics and Structural Biology of the Department of Molecular and Cell Biology (2015–2020). She is a Howard Hughes Medical Institute investigator.
In cell biology, microtubule nucleation is the event that initiates de novo formation of microtubules (MTs). These filaments of the cytoskeleton typically form through polymerization of α- and β-tubulin dimers, the basic building blocks of the microtubule, which initially interact to nucleate a seed from which the filament elongates.
In enzymology, a microtubule-severing ATPase (EC 3.6.4.3) is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha-tubulin N-acetyltransferase is an enzyme which is encoded by the ATAT1 gene.
Katanin p80 WD40-containing subunit B1 is a protein that in humans is encoded by the KATNB1 gene.
Katanin p60 ATPase-containing subunit A1 is an enzyme that in humans is encoded by the KATNA1 gene.
Jennifer Lippincott-Schwartz is a Senior Group Leader at Howard Hughes Medical Institute's Janelia Research Campus and a founding member of the Neuronal Cell Biology Program at Janelia. Previously, she was the Chief of the Section on Organelle Biology in the Cell Biology and Metabolism Program, in the Division of Intramural Research in the Eunice Kennedy Shriver National Institute of Child Health and Human Development at the National Institutes of Health from 1993 to 2016. Lippincott-Schwartz received her PhD from Johns Hopkins University, and performed post-doctoral training with Richard Klausner at the NICHD, NIH in Bethesda, Maryland.
Don W. Cleveland is an American cancer biologist and neurobiologist.
Iva Marija Tolić is a Croatian biophysicist, known for her work on the microtubule cytoskeleton and associated motor proteins. She is currently senior research group leader and professor of biology at the Ruđer Bošković Institute in Zagreb, Croatia.
Calmodulin-regulated spectrin-associated protein family member 2 (CAMSAP2) is a protein in humans that is encoded by the CAMSAP2 gene. CAMSAP2 possesses a microtubule-binding domain near the C-terminal region where "microtubule interactions" occur. On the C-terminal regions, protein to protein interactions are accelerated by three coiled-coil domains, which function as molecular spacers. CAMSAP2 acts as a microtubule minus-end anchor and binds microtubules through its CKK domain. CAMSAP2 is necessary for the proper organization and stabilization of interphase microtubules. The protein also plays a role in cell migration. CAMSAP2 stabilizes and attaches microtubule minus ends to the Golgi through the AKAP9 complex and myomegalin. CLASP1 proteins are responsible for microtubule stability which are not required for the Golgi tethering. When no centromeres are present, AKAP9 and CAMSAP-2 dependent pathways of the microtubule minus ends become a dominant force and must exist in order to observe the maintenance of microtubule density.
Samara Reck-Peterson is an American cell biologist and biophysicist. She is a Professor of Cellular and Molecular Medicine and Cell and Developmental Biology at the University of California, San Diego and an Investigator of the Howard Hughes Medical Institute. She is known for her contributions to our understanding of how dynein, an exceptionally large motor protein that moves many intracellular cargos, works and is regulated. She developed one of the first systems to produce recombinant dynein and discovered that, unlike other cytoskeletal motors, dynein can take a wide variety of step sizes, forward and back and even sideways. She lives in San Diego, California.
Neurotubules are microtubules found in neurons in nervous tissues. Along with neurofilaments and microfilaments, they form the cytoskeleton of neurons. Neurotubules are undivided hollow cylinders that are made up of tubulin protein polymers and arrays parallel to the plasma membrane in neurons. Neurotubules have an outer diameter of about 23 nm and an inner diameter, also known as the central core, of about 12 nm. The wall of a neurotubule is about 5 nm in width. There is a non-opaque clear zone surrounding the neurotubule and it is about 40 nm in diameter. Like microtubules, neurotubules are greatly dynamic and their length can be adjusted by polymerization and depolymerization of tubulin.
Trisha Nell Davis is an American biochemist and the former Earl Davie/ZymoGenetics Chair of the department of biochemistry at the University of Washington. Her early research focused on Calmodulin, though the primary focus of her lab has since shifted to the molecular machinery of cell division in budding yeast, especially the microtubule organizing centers and the kinetochores. She retired in 2024 after 11 years serving as the Chair.
Jonathon (Joe) Howard is a biophysicist and cell biologist. He is the Eugene Higgins Professor of Molecular Biophysics & Biochemistry and a professor of physics at Yale University. His research is focused on microtubules, motor proteins and cell shape and motion.
References
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- 1 2 3 Spencer, Timothy K. (2017-04-13). "Antonina Roll-Mecak: Decoding the secrets of tubulin complexity". Journal of Cell Biology. 216 (5): 1208–1209. doi:10.1083/jcb.201703011. ISSN 0021-9525. PMC 5412576 . PMID 28408403. S2CID 4061992.
- 1 2 3 4 Roll-Mecak, Antonina; Pierce, William (6 June 2016). "ASCB-Gibco Emerging Leader Prize Essay". ascb.org. Retrieved 7 July 2022.
- 1 2 Physics, American Institute of (2021-09-24). "Antonina Roll-Mecak". www.aip.org. Retrieved 2022-06-30.
- 1 2 3 "About Antonina | NINDS Division of Intramural Research". research.ninds.nih.gov. Retrieved 2022-07-05.
- ↑ "NINDS's Roll-Mecak Is 2016 Blavatnik Finalist" (PDF). NIH Record. 68 (23): 10. 4 November 2016 – via nihrecord.nih.gov/.
- ↑ "2023 Award winners". Biochemical Society. Archived from the original on 2022-12-02. Retrieved 2022-07-07.
