AI Article Synopsis

  • Alpha- and beta-tubulin dimers combine to form microtubules, which are crucial for maintaining cell structure and facilitating processes like division and transport.
  • Individual microtubules can vary in their composition of tubulin isotypes and undergo posttranslational modifications, but understanding these variations is currently limited.
  • The study focuses on identifying and quantifying alpha- and beta-tubulin mRNAs and proteins in developing hippocampal neuron cultures and mouse brain tissues, providing insight into tubulin isotype expression during development.

Article Abstract

Alpha- and beta-tubulin dimers polymerize into protofilaments that associate laterally to constitute a hollow tube, the microtubule. A dynamic network of interlinking filaments forms the microtubule cytoskeleton, which maintains the structure of cells and is key to various cellular processes including cell division, cell migration, and intracellular transport. Individual microtubules have an identity that depends on the differential integration of specific alpha- and beta-tubulin isotypes and is further specified by a variety of posttranslational modifications (PTMs). It is barely understood to which extent neighboring microtubules differ in their tubulin composition or whether specific tubulin isotypes cluster along the polymer. Furthermore, our knowledge about the spatio-temporal expression patterns of tubulin isotypes is limited, not at least due to the lack of antibodies or antibody cross-reactivities. Here, we asked which alpha- and beta-tubulin mRNAs and proteins are expressed in developing hippocampal neuron cultures and ex vivo brain tissue lysates. Using heterologous expression of GFP-tubulin fusion proteins, we systematically tested antibody-specificities against various tubulin isotypes. Our data provide quantitative information about tubulin expression levels in the mouse brain and classify tubulin isotypes during pre- and postnatal development.

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Source
http://dx.doi.org/10.1002/dneu.22745DOI Listing

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