Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. / Lin, Tien-chen; Gombos, Linda; Neuner, Annett; Sebastian, Dominik; Olsen, Jesper V; Hrle, Ajla; Benda, Christian; Schiebel, Elmar.

In: P L o S One, Vol. 6, No. 5, 2011, p. e19700.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Lin, T, Gombos, L, Neuner, A, Sebastian, D, Olsen, JV, Hrle, A, Benda, C & Schiebel, E 2011, 'Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function', P L o S One, vol. 6, no. 5, pp. e19700. https://doi.org/10.1371/journal.pone.0019700

APA

Lin, T., Gombos, L., Neuner, A., Sebastian, D., Olsen, J. V., Hrle, A., Benda, C., & Schiebel, E. (2011). Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. P L o S One, 6(5), e19700. https://doi.org/10.1371/journal.pone.0019700

Vancouver

Lin T, Gombos L, Neuner A, Sebastian D, Olsen JV, Hrle A et al. Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. P L o S One. 2011;6(5):e19700. https://doi.org/10.1371/journal.pone.0019700

Author

Lin, Tien-chen ; Gombos, Linda ; Neuner, Annett ; Sebastian, Dominik ; Olsen, Jesper V ; Hrle, Ajla ; Benda, Christian ; Schiebel, Elmar. / Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function. In: P L o S One. 2011 ; Vol. 6, No. 5. pp. e19700.

Bibtex

@article{7287415bcb0c4434bec37314e02f1e67,
title = "Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function",
abstract = "The yeast ¿-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in ¿-tubulins from yeast to human.",
keywords = "Amino Acid Sequence, Amino Acids, Cell Cycle Proteins, Cytoskeletal Proteins, Humans, Indoleacetic Acids, Microbial Viability, Microtubule-Associated Proteins, Microtubules, Mitotic Spindle Apparatus, Molecular Sequence Data, Mutant Proteins, Nuclear Proteins, Phenotype, Phosphorylation, Protein Binding, Protein Subunits, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Tubulin",
author = "Tien-chen Lin and Linda Gombos and Annett Neuner and Dominik Sebastian and Olsen, {Jesper V} and Ajla Hrle and Christian Benda and Elmar Schiebel",
year = "2011",
doi = "10.1371/journal.pone.0019700",
language = "English",
volume = "6",
pages = "e19700",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "5",

}

RIS

TY - JOUR

T1 - Phosphorylation of the yeast γ-tubulin Tub4 regulates microtubule function

AU - Lin, Tien-chen

AU - Gombos, Linda

AU - Neuner, Annett

AU - Sebastian, Dominik

AU - Olsen, Jesper V

AU - Hrle, Ajla

AU - Benda, Christian

AU - Schiebel, Elmar

PY - 2011

Y1 - 2011

N2 - The yeast ¿-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in ¿-tubulins from yeast to human.

AB - The yeast ¿-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in ¿-tubulins from yeast to human.

KW - Amino Acid Sequence

KW - Amino Acids

KW - Cell Cycle Proteins

KW - Cytoskeletal Proteins

KW - Humans

KW - Indoleacetic Acids

KW - Microbial Viability

KW - Microtubule-Associated Proteins

KW - Microtubules

KW - Mitotic Spindle Apparatus

KW - Molecular Sequence Data

KW - Mutant Proteins

KW - Nuclear Proteins

KW - Phenotype

KW - Phosphorylation

KW - Protein Binding

KW - Protein Subunits

KW - Protein Transport

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Tubulin

U2 - 10.1371/journal.pone.0019700

DO - 10.1371/journal.pone.0019700

M3 - Journal article

C2 - 21573187

VL - 6

SP - e19700

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 5

ER -

ID: 40291472