Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.

Mal3p and Tip1p are the fission yeast (Schizosaccharomyces pombe) homologues of EB1 and CLIP-170, two conserved microtubule plus end tracking proteins (+TIPs). These proteins are crucial regulators of microtubule dynamics. Using electron tomography, we carried out a high-resolution analysis of the p...

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Main Authors: Johanna L Höög, Stephen M Huisman, Damian Brunner, Claude Antony
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3627915?pdf=render
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spelling doaj-814ce01eee6c4c1cafa5fd778b7adca32020-11-25T01:55:11ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0184e6169810.1371/journal.pone.0061698Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.Johanna L HöögStephen M HuismanDamian BrunnerClaude AntonyMal3p and Tip1p are the fission yeast (Schizosaccharomyces pombe) homologues of EB1 and CLIP-170, two conserved microtubule plus end tracking proteins (+TIPs). These proteins are crucial regulators of microtubule dynamics. Using electron tomography, we carried out a high-resolution analysis of the phenotypes caused by mal3 and tip1 deletions. We describe the 3-dimensional microtubule organization, quantify microtubule end structures and uncover novel defects of the microtubule lattices. We also reveal unexpected structural modifications of the spindle pole bodies (SPBs), the yeast microtubule organizing centers. In both mutants we observe an increased SPB volume and a reduced number of MT/SPB attachments. The discovered defects alter previous interpretations of the mutant phenotypes and provide new insights into the molecular functions of the two protein families.http://europepmc.org/articles/PMC3627915?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Johanna L Höög
Stephen M Huisman
Damian Brunner
Claude Antony
spellingShingle Johanna L Höög
Stephen M Huisman
Damian Brunner
Claude Antony
Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.
PLoS ONE
author_facet Johanna L Höög
Stephen M Huisman
Damian Brunner
Claude Antony
author_sort Johanna L Höög
title Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.
title_short Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.
title_full Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.
title_fullStr Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.
title_full_unstemmed Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.
title_sort electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +tip mutants.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2013-01-01
description Mal3p and Tip1p are the fission yeast (Schizosaccharomyces pombe) homologues of EB1 and CLIP-170, two conserved microtubule plus end tracking proteins (+TIPs). These proteins are crucial regulators of microtubule dynamics. Using electron tomography, we carried out a high-resolution analysis of the phenotypes caused by mal3 and tip1 deletions. We describe the 3-dimensional microtubule organization, quantify microtubule end structures and uncover novel defects of the microtubule lattices. We also reveal unexpected structural modifications of the spindle pole bodies (SPBs), the yeast microtubule organizing centers. In both mutants we observe an increased SPB volume and a reduced number of MT/SPB attachments. The discovered defects alter previous interpretations of the mutant phenotypes and provide new insights into the molecular functions of the two protein families.
url http://europepmc.org/articles/PMC3627915?pdf=render
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