Characterization of gamma-tubulin filaments in mammalian cells

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Characterization of gamma-tubulin filaments in mammalian cells. / Lindström, Lisa; Alvarado-Kristensson, Maria.

I: Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1865, Nr. 1, 01.01.2018, s. 158-171.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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Lindström, Lisa; Alvarado-Kristensson, Maria / Characterization of gamma-tubulin filaments in mammalian cells.

I: Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1865, Nr. 1, 01.01.2018, s. 158-171.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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TY - JOUR

T1 - Characterization of gamma-tubulin filaments in mammalian cells

AU - Lindström,Lisa

AU - Alvarado-Kristensson,Maria

PY - 2018/1/1

Y1 - 2018/1/1

N2 - Overexpression of γ-tubulin leads to the formation of filaments, but nothing is known about such filaments with regard to possible presence in cells, structure and probable dynamics. Here, we used mammalian cell lines to investigate the ability of γ-tubulin to form filaments. We found that γ-tubulin produces fibers called γ-tubules in a GTP-dependent manner and that γ-tubules are made up of pericentrin and the γ-tubulin complex proteins 2, 3, 5 and 6. Furthermore, we noted that the number of cells with cytosolic γ-tubules is increased in non-dividing cells. Our experiments showed that γ-tubules are polar structures that have a low regrowth rate compared to microtubules. Also, we observed that γ-tubules were disassembled by treatment with cold, colcemid, citral dimethyl acetal, dimethyl fumarate or mutation of γ-tubulin GTPase domain, but were increased in number by treatment with taxol or by stable expression of the γ-tubulin1–333 GTPase domain. Our results demonstrate that γ-tubulin forms filaments, and such assembly is facilitated by the GTPase domain of γ-tubulin.

AB - Overexpression of γ-tubulin leads to the formation of filaments, but nothing is known about such filaments with regard to possible presence in cells, structure and probable dynamics. Here, we used mammalian cell lines to investigate the ability of γ-tubulin to form filaments. We found that γ-tubulin produces fibers called γ-tubules in a GTP-dependent manner and that γ-tubules are made up of pericentrin and the γ-tubulin complex proteins 2, 3, 5 and 6. Furthermore, we noted that the number of cells with cytosolic γ-tubules is increased in non-dividing cells. Our experiments showed that γ-tubules are polar structures that have a low regrowth rate compared to microtubules. Also, we observed that γ-tubules were disassembled by treatment with cold, colcemid, citral dimethyl acetal, dimethyl fumarate or mutation of γ-tubulin GTPase domain, but were increased in number by treatment with taxol or by stable expression of the γ-tubulin1–333 GTPase domain. Our results demonstrate that γ-tubulin forms filaments, and such assembly is facilitated by the GTPase domain of γ-tubulin.

KW - Filaments

KW - γ-Tubulin

KW - γ-Tubulin ring complex

U2 - 10.1016/j.bbamcr.2017.10.008

DO - 10.1016/j.bbamcr.2017.10.008

M3 - Article

VL - 1865

SP - 158

EP - 171

JO - Biochimica et Biophysica Acta - Molecular Cell Research

T2 - Biochimica et Biophysica Acta - Molecular Cell Research

JF - Biochimica et Biophysica Acta - Molecular Cell Research

SN - 0167-4889

IS - 1

ER -