Abstract

Microtubules (MTs), heterodimers of α- and β-tubulin, are involved in different cellular processes including mitosis, cell motility, intracellular transport, cell shape and polarization. In most eukaryotes tubulins, especially the α, are subjected to several post-translational modifications (PTMs) which include acetylation, tyrosination, detyrosination, Δ2 modification, polyglutamylation, that characterize different type of MTs and regulate the interactions between MTs and certain MAPs or motor proteins. Despite neurons, in which presence and distributions of tubulin PTMs are well evaluated, in glial cells like Schwann cells, little is known about the diverse tubulin PTMs amount, distribution and their functional role. So that, the purpose of the present work was to deepen the knowledge about the diverse tubulin PTMs in a commonly used immortalized Schwann cell line. By Western blot analysis we found a higher amount of polyglutamylated and tyrosinated α-tubulin, whereas acetylated, Δ2 and detyrosinated α-tubulin were less expressed. Immunofluorescence staining, highlighted the distribution of acetylated and detyrosinated α-tubulin along the Schwann cells prolongations. In contrast, polyglutamylated α-tubulin was more detectable close to the cell body of Schwann cells, whereas the Δ2-modification was mainly distributed round the nuclear profile. Summing up, our investigation offers insight on several tubulin PTMs amount and distribution in Schwann cells. This could be a further contribution to better understand the role played by different MTs in Schwann cells biology and during the onset of certain disorders of peripheral nervous system.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.