Kinesin superfamily proteins and the regulation of microtubule dynamics in morphogenesis

Niwa, Shinsuke

doi:10.1007/s12565-014-0259-5

Cited by 45 publications

(37 citation statements)

References 57 publications

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“…For instance, KIF11, KIF20A, KIF4A, KIF20B and KIF15 encode proteins of the kinesin superfamily, a group of microtubule-dependent molecular motors. Proteins of the kinesin superfamily provide force for intracellular transport and cell division and are essential for mitosis and meiosis [74]. An important role during mitosis also plays topoisomerase IIα, encoded by the most strongly up-regulated gene TOP2A (2.9-fold), in resolving anaphase bridges between sister chromatids to ensure that daughter cells receive only one copy of each chromosome [75].…”

Section: Discussionmentioning

confidence: 99%

Analysis of hepatic transcript profile and plasma lipid profile in early lactating dairy cows fed grape seed and grape marc meal extract

Geßner

Winkler²,

Koch

et al. 2017

BMC Genomics

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BackgroundIt was recently reported that dairy cows fed a polyphenol-rich grape seed and grape marc meal extract (GSGME) during the transition period had an increased milk yield, but the underlying reasons remained unclear. As polyphenols exert a broad spectrum of metabolic effects, we hypothesized that feeding of GSGME influences metabolic pathways in the liver which could account for the positive effects of GSGME in dairy cows. In order to identify these pathways, we performed genome-wide transcript profiling in the liver and lipid profiling in plasma of dairy cows fed GSGME during the transition period at 1 week postpartum.ResultsTranscriptomic analysis of the liver revealed 207 differentially expressed transcripts, from which 156 were up- and 51 were down-regulated, between cows fed GSGME and control cows. Gene set enrichment analysis of the 155 up-regulated mRNAs showed that the most enriched gene ontology (GO) biological process terms were dealing with cell cycle regulation and the most enriched Kyoto Encyclopedia of Genes and Genomes pathways were p53 signaling and cell cycle. Functional analysis of the 43 down-regulated mRNAs revealed that a great part of these genes are involved in endoplasmic reticulum (ER) stress-induced unfolded protein response (UPR) and inflammatory processes. Accordingly, protein folding, response to unfolded protein, unfolded protein binding, chemokine activity and heat shock protein binding were identified as one of the most enriched GO biological process and molecular function terms assigned to the down-regulated genes. In line with the transcriptomics data the plasma concentrations of the acute phase proteins serum amyloid A (SAA) and haptoglobin were reduced in cows fed GSGME compared to control cows. Lipidomic analysis of plasma revealed no differences in the concentrations of individual species of major and minor lipid classes between cows fed GSGME and control cows.ConclusionsAnalysis of hepatic transcript profile in cows fed GSGME during the transition period at 1 week postpartum indicates that polyphenol-rich feed components are able to inhibit ER stress-induced UPR and inflammatory processes, both of which are considered to contribute to liver-associated diseases and to impair milk performance in dairy cows, in the liver of dairy cows during early lactation.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-017-3638-1) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Analysis of hepatic transcript profile and plasma lipid profile in early lactating dairy cows fed grape seed and grape marc meal extract

Geßner

Winkler²,

Koch

et al. 2017

BMC Genomics

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“…Many proteins termed microtubule destabilizers actually promote microtubule disassembly, and would be more accurately termed microtubule depolymerizers. Examples are stathmin and its neuron‐specific variant called SCG10, which shift microtubules toward disassembly by sequestering tubulin subunits and by promoting catastrophe, as well as certain “depolymerizing” kinesins (kinesin‐8 and kinesin‐13) that use the forces of ATP hydrolysis to tear subunits from the ends of microtubules [Chauvin and Sobel, ; Niwa, ]. By depolymerizing the labile domains of microtubules, such proteins would reduce the total microtubule mass and shift the microtubule array to a greater proportion of the total being stable.…”

Section: Factors That Affect Microtubule Stability In the Neuronmentioning

confidence: 99%

Stability properties of neuronal microtubules

et al. 2016

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Neurons are terminally differentiated cells that use their microtubule arrays not for cell division but rather as architectural elements required for the elaboration of elongated axons and dendrites. In addition to acting as compression-bearing struts that provide for the shape of the neuron, microtubules also act as directional railways for organelle transport. The stability properties of neuronal microtubules are commonly discussed in the biomedical literature as crucial to the development and maintenance of the nervous system, and have recently gained attention as central to the etiology of neurodegenerative diseases. Drugs that affect microtubule stability are currently under investigation as potential therapies for disease and injury of the nervous system. There is often a lack of consistency, however, in how the issue of microtubule stability is discussed in the literature, and this can affect the design and interpretation of experiments as well as potential therapeutic regimens. Neuronal microtubules are considered to be more stable than microtubules in dividing cells. On average, this is true, but in addition to an abundant stable microtubule fraction in neurons, there is also an abundant labile microtubule fraction. Both are functionally important. Individual microtubules consist of domains that differ in their stability properties, and these domains can also differ markedly in their composition as well as how they interact with various microtubule-related proteins in the neuron. Myriad proteins and pathways have been discussed as potential contributors to microtubule stability in neurons.

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“…Examples are stathmin and its neuron-specific variant called SCG10, which shift microtubules toward disassembly by sequestering tubulin subunits and by promoting catastrophe, as well as certain “depolymerizing” kinesins (kinesin-8 and kinesin-13) that use the forces of ATP hydrolysis to remove tubulin subunits from the ends of microtubules (49, 50). Fidgetin, a novel microtubule severing protein, appears to target labile domains of microtubules, creating short microtubule fragments that quickly depolymerize into free tubulin (51).…”

Section: Microtubule Dynamics and Stability In Neuronsmentioning

confidence: 99%

Microtubules in health and degenerative disease of the nervous system

Matamoros

Baas

2016

Brain Research Bulletin

112

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Microtubules are essential for the development and maintenance of axons and dendrites throughout the life of the neuron, and are vulnerable to degradation and disorganization in a variety of neurodegenerative diseases. Microtubules, polymers of tubulin heterodimers, are intrinsically polar structures with a plus end favored for assembly and disassembly and a minus end less favored for these dynamics. In the axon, microtubules are nearly uniformly oriented with plus ends out, whereas in dendrites, microtubules have mixed orientations. Microtubules in developing neurons typically have a stable domain toward the minus end and a labile domain toward the plus end. This domain structure becomes more complex during neuronal maturation when especially stable patches of polyaminated tubulin become more prominent within the microtubule. Microtubules are the substrates for molecular motor proteins that transport cargoes toward the plus or minus end of the microtubule, with motor-driven forces also responsible for organizing microtubules into their distinctive polarity patterns in axons and dendrites. A vast array of microtubule-regulatory proteins impart direct and indirect changes upon the microtubule arrays of the neuron, and these include microtubule-severing proteins as well as proteins responsible for the stability properties of the microtubules. During neurodegenerative diseases, microtubule mass is commonly diminished, and the potential exists for corruption of the microtubule polarity patterns and microtubule-mediated transport. These ill effects may be a primary causative factor in the disease or may be secondary effects, but regardless, therapeutics capable of correcting these microtubule abnormalities have great potential to improve the status of the degenerating nervous system.

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Kinesin superfamily proteins and the regulation of microtubule dynamics in morphogenesis

Cited by 45 publications

References 57 publications

Analysis of hepatic transcript profile and plasma lipid profile in early lactating dairy cows fed grape seed and grape marc meal extract

Analysis of hepatic transcript profile and plasma lipid profile in early lactating dairy cows fed grape seed and grape marc meal extract

Stability properties of neuronal microtubules

Microtubules in health and degenerative disease of the nervous system

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