Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism

Frauke Hussmann, Douglas Robert Drummond, Daniel R. Peet, Douglas S. Martin, Robert A. Cross

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

Alp14 is a TOG-family microtubule polymerase from S. pombe that tracks plus ends and accelerates their growth. To interrogate its mechanism, we reconstituted dynamically unstable single isoform S. pombe microtubules with full length Alp14/TOG and Alp7, the TACC-family binding partner of Alp14. We find that Alp14 can drive microtubule plus end growth at GTP-tubulin concentrations at least 10-fold below the usual critical concentration, at the expense of increased catastrophe. This reveals Alp14 to be a highly unusual enzyme that biases the equilibrium for the reaction that it catalyses. Alp7/TACC enhances the effectiveness of Alp14, by increasing its occupancy. Consistent with this, we show in live cells that Alp7 deletion produces very similar MT dynamics defects to Alp14 deletion. The ability of Alp7/14 to accelerate and bias GTP-tubulin exchange at microtubule plus ends allows it to generate long-lived, fast-growing microtubules at very low cellular free tubulin concentrations.

元の言語英語
記事番号20653
ジャーナルScientific reports
6
DOI
出版物ステータス出版済み - 2 11 2016

Fingerprint

Microtubules
Tubulin
Schizosaccharomyces
Guanosine Triphosphate
Growth
Protein Isoforms
Enzymes

All Science Journal Classification (ASJC) codes

  • General

これを引用

Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism. / Hussmann, Frauke; Drummond, Douglas Robert; Peet, Daniel R.; Martin, Douglas S.; Cross, Robert A.

:: Scientific reports, 巻 6, 20653, 11.02.2016.

研究成果: ジャーナルへの寄稿記事

Hussmann, Frauke ; Drummond, Douglas Robert ; Peet, Daniel R. ; Martin, Douglas S. ; Cross, Robert A. / Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism. :: Scientific reports. 2016 ; 巻 6.
@article{5c916e60ff824c8587faa0b0920a51a1,
title = "Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism",
abstract = "Alp14 is a TOG-family microtubule polymerase from S. pombe that tracks plus ends and accelerates their growth. To interrogate its mechanism, we reconstituted dynamically unstable single isoform S. pombe microtubules with full length Alp14/TOG and Alp7, the TACC-family binding partner of Alp14. We find that Alp14 can drive microtubule plus end growth at GTP-tubulin concentrations at least 10-fold below the usual critical concentration, at the expense of increased catastrophe. This reveals Alp14 to be a highly unusual enzyme that biases the equilibrium for the reaction that it catalyses. Alp7/TACC enhances the effectiveness of Alp14, by increasing its occupancy. Consistent with this, we show in live cells that Alp7 deletion produces very similar MT dynamics defects to Alp14 deletion. The ability of Alp7/14 to accelerate and bias GTP-tubulin exchange at microtubule plus ends allows it to generate long-lived, fast-growing microtubules at very low cellular free tubulin concentrations.",
author = "Frauke Hussmann and Drummond, {Douglas Robert} and Peet, {Daniel R.} and Martin, {Douglas S.} and Cross, {Robert A.}",
year = "2016",
month = "2",
day = "11",
doi = "10.1038/srep20653",
language = "English",
volume = "6",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism

AU - Hussmann, Frauke

AU - Drummond, Douglas Robert

AU - Peet, Daniel R.

AU - Martin, Douglas S.

AU - Cross, Robert A.

PY - 2016/2/11

Y1 - 2016/2/11

N2 - Alp14 is a TOG-family microtubule polymerase from S. pombe that tracks plus ends and accelerates their growth. To interrogate its mechanism, we reconstituted dynamically unstable single isoform S. pombe microtubules with full length Alp14/TOG and Alp7, the TACC-family binding partner of Alp14. We find that Alp14 can drive microtubule plus end growth at GTP-tubulin concentrations at least 10-fold below the usual critical concentration, at the expense of increased catastrophe. This reveals Alp14 to be a highly unusual enzyme that biases the equilibrium for the reaction that it catalyses. Alp7/TACC enhances the effectiveness of Alp14, by increasing its occupancy. Consistent with this, we show in live cells that Alp7 deletion produces very similar MT dynamics defects to Alp14 deletion. The ability of Alp7/14 to accelerate and bias GTP-tubulin exchange at microtubule plus ends allows it to generate long-lived, fast-growing microtubules at very low cellular free tubulin concentrations.

AB - Alp14 is a TOG-family microtubule polymerase from S. pombe that tracks plus ends and accelerates their growth. To interrogate its mechanism, we reconstituted dynamically unstable single isoform S. pombe microtubules with full length Alp14/TOG and Alp7, the TACC-family binding partner of Alp14. We find that Alp14 can drive microtubule plus end growth at GTP-tubulin concentrations at least 10-fold below the usual critical concentration, at the expense of increased catastrophe. This reveals Alp14 to be a highly unusual enzyme that biases the equilibrium for the reaction that it catalyses. Alp7/TACC enhances the effectiveness of Alp14, by increasing its occupancy. Consistent with this, we show in live cells that Alp7 deletion produces very similar MT dynamics defects to Alp14 deletion. The ability of Alp7/14 to accelerate and bias GTP-tubulin exchange at microtubule plus ends allows it to generate long-lived, fast-growing microtubules at very low cellular free tubulin concentrations.

UR - http://www.scopus.com/inward/record.url?scp=84958559089&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84958559089&partnerID=8YFLogxK

U2 - 10.1038/srep20653

DO - 10.1038/srep20653

M3 - Article

VL - 6

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 20653

ER -