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The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization

Lindström, Lisa LU ; Li, Tongbin; Malycheva, Darina LU ; Kancharla, Arun; Nilsson, Helén LU ; Vishnu, Neelanjan LU ; Mulder, Hindrik LU ; Johansson, Martin LU ; Rosselló, Catalina Ana and Alvarado-Kristensson, Maria LU (2018) In Communications Biology 1(https://doi.org/10.1038/s42003-018-0037-3).
Abstract (Swedish)
In the cell, γ-tubulin establishes a cellular network of threads named the γ-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that γ-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that γ-tubulin has a role in the maintenance of the mitochondrial network and functions as reduced levels of γ-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of γ-tubulin DNA-binding domain enhanced the association of γ-tubulin with... (More)
In the cell, γ-tubulin establishes a cellular network of threads named the γ-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that γ-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that γ-tubulin has a role in the maintenance of the mitochondrial network and functions as reduced levels of γ-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of γ-tubulin DNA-binding domain enhanced the association of γ-tubulin with mitochondria. Our results demonstrate that γ-tubulin is an important mitochondrial structural component that maintains the mitochondrial network, providing mitochondria with a cellular infrastructure. We propose that γ-tubulin provides a cytoskeletal element that gives form to the mitochondrial network. (Less)
Abstract
In the cell, γ-tubulin establishes a cellular network of threads named the γ-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that γ-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that γ-tubulin has a role in the maintenance of the mitochondrial network and functions as reduced levels of γ-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of γ-tubulin DNA-binding domain enhanced the association of γ-tubulin with... (More)
In the cell, γ-tubulin establishes a cellular network of threads named the γ-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that γ-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that γ-tubulin has a role in the maintenance of the mitochondrial network and functions as reduced levels of γ-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of γ-tubulin DNA-binding domain enhanced the association of γ-tubulin with mitochondria. Our results demonstrate that γ-tubulin is an important mitochondrial structural component that maintains the mitochondrial network, providing mitochondria with a cellular infrastructure. We propose that γ-tubulin provides a cytoskeletal element that gives form to the mitochondrial network. (Less)
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organization
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Contribution to journal
publication status
published
subject
in
Communications Biology
volume
1
issue
https://doi.org/10.1038/s42003-018-0037-3
publisher
Nature Research
ISSN
2399-3642
DOI
10.1038/s42003-018-0037-3
language
English
LU publication?
yes
id
1a191f20-68d3-4f6c-b672-08f529a97c71
date added to LUP
2018-08-27 13:37:47
date last changed
2018-12-05 03:00:18
@article{1a191f20-68d3-4f6c-b672-08f529a97c71,
  abstract     = {In the cell, γ-tubulin establishes a cellular network of threads named the γ-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that γ-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that γ-tubulin has a role in the maintenance of the mitochondrial network and functions as reduced levels of γ-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of γ-tubulin DNA-binding domain enhanced the association of γ-tubulin with mitochondria. Our results demonstrate that γ-tubulin is an important mitochondrial structural component that maintains the mitochondrial network, providing mitochondria with a cellular infrastructure. We propose that γ-tubulin provides a cytoskeletal element that gives form to the mitochondrial network.},
  articleno    = {37},
  author       = {Lindström, Lisa and Li, Tongbin and Malycheva, Darina and Kancharla, Arun and Nilsson, Helén and Vishnu, Neelanjan and Mulder, Hindrik and Johansson, Martin and Rosselló, Catalina Ana and Alvarado-Kristensson, Maria},
  issn         = {2399-3642},
  language     = {eng},
  month        = {05},
  number       = {https://doi.org/10.1038/s42003-018-0037-3},
  publisher    = {Nature Research},
  series       = {Communications Biology},
  title        = {The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization},
  url          = {http://dx.doi.org/10.1038/s42003-018-0037-3},
  volume       = {1},
  year         = {2018},
}