The influence of light on microtubule dynamics and alignment in the Arabidopsis hypocotyl.

Plant Cell

Department of Cell and Developmental Biology, John Ines Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.

Published: January 2012

Light and dark have antagonistic effects on shoot elongation, but little is known about how these effects are translated into changes of shape. Here we provide genetic evidence that the light/gibberellin-signaling pathway affects the properties of microtubules required to reorient growth. To follow microtubule dynamics for hours without triggering photomorphogenic inhibition of growth, we used Arabidopsis thaliana light mutants in the gibberellic acid/DELLA pathway. Particle velocimetry was used to map the mass movement of microtubule plus ends, providing new insight into the way that microtubules switch between orthogonal axes upon the onset of growth. Longitudinal microtubules are known to signal growth cessation, but we observed that cells also self-organize a strikingly bipolarized longitudinal array before bursts of growth. This gives way to a radial microtubule star that, far from being a random array, seems to be a key transitional step to the transverse array, forecasting the faster elongation that follows. Computational modeling provides mechanistic insight into these transitions. In the faster-growing mutants, the microtubules were found to have faster polymerization rates and to undergo faster reorientations. This suggests a mechanism in which the light-signaling pathway modifies the dynamics of microtubules and their ability to switch between orthogonal axes.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3289555PMC
http://dx.doi.org/10.1105/tpc.111.093849DOI Listing

Publication Analysis

Top Keywords

microtubule dynamics
8
switch orthogonal
8
orthogonal axes
8
microtubules
5
growth
5
influence light
4
microtubule
4
light microtubule
4
dynamics alignment
4
alignment arabidopsis
4

Similar Publications

We analysed here the dynamic of the kinesin-like Pavarotti (Pav) during male gametogenesis of wild-type and Sas4 mutant flies. Pav localizes to the equatorial region and the inner central spindle of late anaphase wild-type spermatogonia and displays a strong concentration at the midbody during late telophase. At metaphase of the first meiotic division, Pav shows widespread localization on the equatorial region of the spermatocytes.

View Article and Find Full Text PDF

Klp2-mediated Rsp1-Mto1 colocalization inhibits microtubule-dependent microtubule assembly in fission yeast.

Sci Adv

January 2025

MOE Key Laboratory for Cellular Dynamics and Center for Advanced Interdisciplinary Science and Biomedicine of IHM, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, 230027, China.

Microtubule assembly takes place at the centrosome and noncentrosomal microtubule-organizing centers (MTOCs). However, the mechanisms controlling the activity of noncentrosomal MTOCs are poorly understood. Here, using the fission yeast as a model organism, we demonstrate that the kinesin-14 motor Klp2 interacts with the J-domain Hsp70/Ssa1 cochaperone Rsp1, an inhibitory factor of microtubule assembly, and that Klp2 is required for the proper localization of Rsp1 to microtubules.

View Article and Find Full Text PDF

Basic Science and Pathogenesis.

Alzheimers Dement

December 2024

University of Pittsburgh School of Pharmacy, Pittsburgh, PA, USA.

Background: Reversible post-translational modifications, phosphorylation and dephosphorylation, on tau protein play a critical role in the microtubule (MT) modulation. However, abnormal tau phosphorylation, which occurs in tauopathies such as Alzheimer's disease (AD), causes the dissociation of tau from MTs. The dissociated tau then aggregates into sequent forms from soluble oligomers to paired helical filaments (PHF), and insoluble neurofibrillary tangles (NFTs), a hallmark of AD.

View Article and Find Full Text PDF

Background: Tauopathies, including Alzheimer's Disease and Frontotemporal Dementia, are characterized as intracellular lesions composed of aggregated tau proteins. Soluble tau oligomers are shown to be one of the most toxic species and are responsible for the spread of tau pathology. Recent studies have found that several proteins such as amyloid b, a-synuclein, and TDP-43 can aggregate tau.

View Article and Find Full Text PDF

Background: In tauopathies, such as Frontotemporal Dementia (FTD), tau loses association with microtubules (MTs) and forms neurofibrillary tangles. Tau is an abundant MT-associated protein in neurons, which essentially regulate MT properties. Because pathological tau binds less avidly to MTs, which was thought to reduce the levels and stability of axonal MTs.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!