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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.

Although the tubulin carboxypeptidase has yet to be identified, its activity was first identified in the late 1970s.[2] 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,[3] which acts only on alpha-tubulin monomer. Since the majority of microtubules are very dynamic, they do not contain much detyrosinated tubulin.

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  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. ^ 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. 
  3. ^ 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 2119537Freely accessible. PMID 8093886.