Tubulin

Tubulin is one of several members of a small family of globular proteins. The most common members of the tubulin family are α-tubulin and β-tubulin, the proteins that make up microtubules. Each has a molecular weight of approximately 50 kDa. These are both part of the larger tubulin superfamily, which also includes five other proteins. Microtubules are assembled from dimers of α- and β-tubulin.

Structure

Tubulin is characterized by the presence of a tubulin domain, which binds GTP and is involved in microtubule assembly. The tubulin domain is found in all members of the tubulin superfamily, which includes α-, β-, and γ-tubulin, as well as several other proteins.

Function

Microtubules, composed of α- and β-tubulin dimers, are involved in many essential cellular processes, including mitosis and meiosis, intracellular transport, and the maintenance of cell shape. γ-Tubulin is found at the microtubule organizing center (MTOC), where it is involved in the nucleation of microtubules.

Clinical significance

Mutations in tubulin genes can lead to various human diseases, including lissencephaly and polyneuropathy. In addition, tubulin interacts with several drugs, including taxol, vinblastine, and colchicine, which interfere with microtubule function and are used in cancer treatment.

See also

• Microtubule
• Mitosis
• Meiosis
• Lissencephaly
• Polyneuropathy

References

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