Ontology highlight
ABSTRACT:
SUBMITTER: Shida T
PROVIDER: S-EPMC3003046 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Shida Toshinobu T Cueva Juan G JG Xu Zhenjie Z Goodman Miriam B MB Nachury Maxence V MV
Proceedings of the National Academy of Sciences of the United States of America 20101110 50
Long-lived microtubules found in ciliary axonemes, neuronal processes, and migrating cells are marked by α-tubulin acetylation on lysine 40, a modification that takes place inside the microtubule lumen. The physiological importance of microtubule acetylation remains elusive. Here, we identify a BBSome-associated protein that we name αTAT1, with a highly specific α-tubulin K40 acetyltransferase activity and a catalytic preference for microtubules over free tubulin. In mammalian cells, the catalyt ...[more]