Detyrosination

Detyrosination is a form of posttranslational modification that occurs on alpha-tubulin.[1] It consists of the removal of the C-terminal tyrosine to expose a glutamate at the newly formed C-terminus. Tubulin polymers, called microtubules, that contain detyrosinated alpha-tubulin are usually referred to as Glu-microtubules while unmodified polymers are called Tyr-microtubules.

The tubulin carboxypeptidases that cleave the terminal tyrosine are two proteases called vashohibins (VASH1/VASH2), in complex with a small protein SVBP that acts as stabilising chaperon.[2] The detyrosynating activity was first identified in the late 1970s.[3] It is a slow acting enzyme that uses polymeric tubulin as a substrate. As a result, only stabilized microtubules accumulate this particular modification. Tubulin detyrosination is reversed by the tubulin-tyrosine ligase,[4] which acts only on alpha-tubulin monomer. Since the majority of microtubules are very dynamic, they do not contain much detyrosinated tubulin.

See also

References

  1. ↑ Janke C, Bulinski JC (2011). "Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions". Nat Rev Mol Cell Biol. 12 (12): 773–86. doi:10.1038/nrm3227. PMID 22086369.
  2. ↑ Nieuwenhuis, Joppe; Adamopoulos, Athanassios; Bleijerveld, Onno B.; Mazouzi, Abdelghani; Stickel, Elmer; Celie, Patrick; Altelaar, Maarten; Knipscheer, Puck; Perrakis, Anastassis (2017-11-16). "Vasohibins encode tubulin detyrosinating activity". Science: eaao5676. doi:10.1126/science.aao5676. ISSN 0036-8075. PMID 29146869.
  3. ↑ Hallak ME, Rodriguez JA, Barra HS, Caputto R (1977). "Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin". FEBS Lett. 73 (2): 147–50. doi:10.1016/0014-5793(77)80968-x. PMID 838053.
  4. ↑ Ersfeld K, Wehland J, Plessmann U, Dodemont H, Gerke V, Weber K (1993). "Characterization of the tubulin-tyrosine ligase". J Cell Biol. 120 (3): 725–32. doi:10.1083/jcb.120.3.725. PMC 2119537. PMID 8093886.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.