What is it?γ-Tubulin is a member of the tubulin superfamily and is required for nucleating the polymerization of microtubules in vivo. Microtubules are dynamic cytoskeletal polymers that assemble from two other members of the tubulin superfamily, α-tubulin and β-tubulin. Microtubules make up the mitotic and meiotic spindles, and are important for establishing cell polarity and vesicle trafficking. The tubulin superfamily is still growing, and now includes tubulins δ through η (delta through eta, in case you've forgotten your Greek). α-, β- and γ-tubulin are conserved in all eukaryotic groups, whereas the other superfamily members are not.How was it found?γ-Tubulin was identified by Oakley and colleagues as a suppressor of a β-tubulin mutation in Aspergillus nidulans.Where is it?γ-Tubulin does not assemble into microtubules. In most cells it is found at the microtubule organizing center, an organelle devoted to microtubule nucleation and anchoring. In animal cells the organizing center is called the centrosome, in fungi it is called the spindle pole body, and in plants it isn't called anything because plants make do without a discrete organizing center. The centrosome consists of a pair of centrioles — microtubule structures with beautiful nine-fold symmetry – surrounded by pericentriolar material. The pericentriolar material nucleates microtubules and contains γ-tubulin. In fungi too γ-tubulin is associated with the surfaces of the spindle pole body that nucleate microtubles. Although γ-tubulin is thought to act primarily at the organizing center, in most cells the majority of γ-tubulin is in the cytoplasm.What's it good for?γ-Tubulin nucleates microtubules, allowing cells to control when and where microtubules polymerize. This has been shown both in vivo, by interfering with γ-tubulin function, and in vitro, by assaying the activity of γ-tubulin. Analysis of γ-tubulin mutants in fungi suggests that γ-tubulin might also have an independent role in cell cycle control.Does it act alone? No. When purified from animal cells, γ-tubulin is a large complex with a molecular weight of several million daltons. In addition to γ-tubulin there are at least five other proteins in this complex, all of which are related to each other and are conserved in animals and plants. We call these proteins the GCPs (gamma-tubulin complex proteins), although there are several other names in the literature. Remarkably, yeast lacks all but two of the GCPs; those GCPs and γ-tubulin form a much smaller complex than that found in animal cells.Size and shape matter! Microtubules are complex polymers, with approximately 13 protofilaments arranged into a tube. The γ-tubulin complex has a size and shape that is very similar to that of a microtubule end, suggesting that it serves as a template for microtubule assembly. The γ-tubulin complex as purified from several organisms is a ring of approximately 25 nm in diameter made up of repeating subunits, with a cap structure on one end, and is often called the γ-tubulin ring complex (γTuRC). The current model for how all the proteins fit together is that the repeating subunit in the ring is γ-tubulin plus the two GCPs that are conserved in all eukaryotes, and that the cap structure is made up of the other GCPs.Getting attached to γ-tubulin Most microtubules grow from the centrosome, so there must be a way to attach the γ-tubulin complex to the centrosome. Although it is not clear how it works, this attachment is likely to be regulated in the cell cycle. The amount of γ-tubulin at the centrosome increases dramatically at the beginning of mitosis, aiding in the formation of the mitotic spindle, then decreases at the end of mitosis. Attachment of the γ-tubulin complex to the nascent centrosome is also an important part of fertilization in most animals since the sperm supplies the centrioles and the egg supplies the γ-tubulin complex; it is only after they get together that the first centrosome is formed and development proceeds.Where can I find out more?
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