Chlamydomonasas a tool to study tubulin polyglutamylation
Author(s) -
Tomohiro Kubo,
Toshiyuki Oda
Publication year - 2018
Publication title -
microscopy
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.545
H-Index - 52
eISSN - 2050-5701
pISSN - 2050-5698
DOI - 10.1093/jmicro/dfy044
Subject(s) - microtubule , chlamydomonas reinhardtii , tubulin , chlamydomonas , acetylation , flagellum , microbiology and biotechnology , biology , intracellular , chemistry , biochemistry , gene , mutant
The diversity of α- and β-tubulin is facilitated by various post-translational modifications (PTMs), such as acetylation, tyrosination, glycylation, glutamylation, phosphorylation and methylation. These PTMs affect the stability and structure of microtubules as well as the interaction between microtubules and microtubule-associated proteins, including molecular motors. Therefore, it is extremely important to investigate the roles of tubulin PTMs for understanding the cell cycle, cell motility and intracellular trafficking. Tubulin PTMs were first studied in the 1980s, and considerable progress has been made since then; it is likely that additional mechanisms remain yet to be elucidated. Here, we discuss one such modification, tubulin glutamylation, and introduce our research on the eukaryotic flagellum of the unicellular green alga Chlamydomonas reinhardtii.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom