Doublecortin is a developmentally regulated, microtubule-associated protein expressed in migrating and differentiating neurons.

Cells generate distinct microtubule subtypes by expressing different tubulin isotypes and through tubulin post-translational modifications, such as detyrosination, acetylation, polyglutamylation and polyglycylation The recent discovery of enzymes responsible for many of these modifications has shown how they may regulate microtubule functions

Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions

Plk4-Induced Centriole Biogenesis in Human Cells

Tubulin, the subunit protein of microtubules, is an alpha/beta heterodimer. In many organisms, both alpha and beta exist in numerous isotypic forms encoded by different genes. In addition, both alpha and beta undergo a variety of posttranslational covalent modifications, including acetylation, phosphorylation, detyrosylation, polyglutamylation, and polyglycylation. In this review the distribution and possible functional significance of the various forms of tubulin are discussed. In analyzing the differences among tubulin isotypes encoded by different genes, some appear to have no functional significance, some increase the overall adaptability of the organism to environmental challenges, and some appear to perform specific functions including formation of particular organelles and interactions with specific proteins. Purified isotypes also display different properties in vitro. Although the significance of all the covalent modification of tubulin is not fully understood, some of them may influence the stability of modified microtubules in vivo as well as interactions with certain proteins and may help to determine the functional role of microtubules in the cell. The review also discusses isotypes of gamma-tubulin and puts various forms of tubulin in an evolutionary context.

Multiple forms of tubulin: different gene products and covalent modifications.

Mutations in the LIS1 gene cause gross histological disorganization of the developing human brain, resulting in a brain surface that is almost smooth. Here we show that LIS1 protein co-immunoprecipitates with cytoplasmic dynein and dynactin, and localizes to the cell cortex and to mitotic kinetochores, which are known sites for binding of cytoplasmic dynein. Overexpression of LIS1 in cultured mammalian cells interferes with mitotic progression and leads to spindle misorientation. Injection of anti-LIS1 antibody interferes with attachment of chromosomes to the metaphase plate, and leads to chromosome loss. We conclude that LIS1 participates in a subset of dynein functions, and may regulate the division of neuronal progenitor cells in the developing brain.

A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein function

Distribution of glutamylated alpha and beta-tubulin in mouse tissues using a specific monoclonal antibody, GT335.

Structure of the polyglutamyl chain of tubulin: occurrence of alpha and gamma linkages between glutamyl units revealed by monoreactive polyclonal antibodies.

The aminoterminal domain of alpha-tubulin probed by monoclonal antibodies. Recognition of a rarely exposed epitope by the monoclonal antibody 111 B52 C2.

D. Chillet

Papers

Distribution of glutamylated alpha and beta-tubulin in mouse tissues using a specific monoclonal antibody, GT335.

Structure of the polyglutamyl chain of tubulin: occurrence of alpha and gamma linkages between glutamyl units revealed by monoreactive polyclonal antibodies.

The aminoterminal domain of alpha-tubulin probed by monoclonal antibodies. Recognition of a rarely exposed epitope by the monoclonal antibody 111 B52 C2.