Format

Send to

Choose Destination
PLoS One. 2012;7(10):e48204. doi: 10.1371/journal.pone.0048204. Epub 2012 Oct 26.

Luminal localization of α-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules.

Author information

1
Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI, USA.

Abstract

The αβ-tubulin subunits of microtubules can undergo a variety of evolutionarily-conserved post-translational modifications (PTMs) that provide functional specialization to subsets of cellular microtubules. Acetylation of α-tubulin residue Lysine-40 (K40) has been correlated with increased microtubule stability, intracellular transport, and ciliary assembly, yet a mechanistic understanding of how acetylation influences these events is lacking. Using the anti-acetylated tubulin antibody 6-11B-1 and electron cryo-microscopy, we demonstrate that the K40 acetylation site is located inside the microtubule lumen and thus cannot directly influence events on the microtubule surface, including kinesin-1 binding. Surprisingly, the monoclonal 6-11B-1 antibody recognizes both acetylated and deacetylated microtubules. These results suggest that acetylation induces structural changes in the K40-containing loop that could have important functional consequences on microtubule stability, bending, and subunit interactions. This work has important implications for acetylation and deacetylation reaction mechanisms as well as for interpreting experiments based on 6-11B-1 labeling.

PMID:
23110214
PMCID:
PMC3482196
DOI:
10.1371/journal.pone.0048204
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Public Library of Science Icon for PubMed Central
Loading ...
Support Center