Polyglutamylation: a fine-regulator of protein function? 'Protein Modifications: beyond the usual suspects' review series.
Polyglutamylation is a post-translational modification in which glutamate side chains of variable lengths are formed on the modified protein. It is evolutionarily conserved from protists to mammals and its most prominent substrate is tubulin, the microtubule (MT) building block. Various polyglutamylation states of MTs can be distinguished within a single cell and they are also characteristic of specific cell types or organelles. Polyglutamylation has been proposed to be involved in the functional adaptation of MTs, as it occurs within the carboxy-terminal tubulin tails that participate directly in the binding of many structural and motor MT-associated proteins. The discovery of a new family of enzymes that catalyse this modification has brought new insight into the mechanism of polyglutamylation and now allows for direct functional studies of the role of tubulin polyglutamylation. Moreover, the recent identification of new substrates of polyglutamylation indicates that this post-translational modification could be a potential regulator of diverse cellular processes.
Centre de Recherches de Biochimie Macromoléculaire, Centre National de la Recherche Scientifique, University Montpellier 2 and 1, 1919 Route de Mende, 34293 Montpellier, France. carsten.janke@crbm.cnrs.fr
Carsten
C
Janke
Krzysztof
K
Rogowski
Juliette
J
van Dijk
D000818:Animals; D006801:Humans; D008870:Microtubules / Q000378:metabolism; D011099:Polyglutamic Acid / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism
D011506:Proteins; D014404:Tubulin; D011099:Polyglutamic Acid