Results 61 to 70 of about 335,784 (179)

CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation

bioRxiv, 2020
Microtubule (MT) nucleation is regulated by the γ-tubulin ring complex (γTuRC), conserved from yeast to humans. In Saccharomyces cerevisiae, γTuRC is composed of seven identical γ-tubulin small complex (γTuSC) sub-assemblies which associate helically to ...
A. Brilot, A. Lyon, A. Zelter, Shruthi Viswanath, A. Maxwell, M. MacCoss, E. Muller, A. Sali, T. Davis, D. Agard   +9 more
semanticscholar   +1 more source

Promiscuous Binding of Microprotein Mozart1 to γ-Tubulin Complex Mediates Specific Subcellular Targeting to Control Microtubule Array Formation

Cell Reports, 2020
Summary: How γ-tubulin ring complex (γ-TuRC), a master template for microtubule nucleation, is spatially and temporally regulated for the assembly of new microtubule arrays remains unclear.
Tzu-Lun Huang, Hsiu-Jung Wang, Ya-Chieh Chang, Shao-Win Wang, Kuo-Chiang Hsia   +4 more
doaj   +1 more source

Cytoskeleton: Microtubule nucleation takes shape [PDF]

Current Biology, 1996
The centrosomal protein gamma-tubulin is part of a ring-shaped complex that can induce microtubule polymerization. This complex may explain how the centrosome nucleates microtubule polymerization, and thereby organizes the microtubule cytoskeleton.
Murphy, Steven M, Stearns, Tim
openaire   +2 more sources

Chemically Fueled Systems Chemistry Across Length Scales

Advanced Functional Materials, EarlyView.
Chemically fueled reaction cycles regulate processes through single and multiple catalytic sites on the molecular and assembly scale. This gives rise to unique kinetically controlled properties/functions like spatio‐temporal catalysis, oscillations, optical properties, and perform work.
Brigitte A. K. Kriebisch, Job Boekhoven
wiley   +1 more source

HURP facilitates spindle assembly by stabilizing microtubules and working synergistically with TPX2

Nature Communications
In vertebrate spindles, most microtubules are formed via branching microtubule nucleation, whereby microtubules nucleate along the side of pre-existing microtubules.
Venecia Alexandria Valdez, Meisheng Ma, Bernardo Gouveia, Rui Zhang, Sabine Petry   +4 more
doaj   +1 more source

Monomeric γ-Tubulin Nucleates Microtubules [PDF]

Journal of Biological Chemistry, 2000
gamma-Tubulin is required for nucleation and polarized organization of microtubules in vivo. The mechanism of microtubule nucleation by gamma-tubulin and the role of associated proteins is not understood. Here we show that in vitro translated monomeric gamma-tubulin nucleates microtubules by lowering the size of the nucleus from seven to three tubulin ...
R, Leguy, R, Melki, D, Pantaloni, M F, Carlier   +3 more
openaire   +2 more sources

Harnessing Phase Separation for the Development of High‐Performance Hydrogels

Advanced Science, EarlyView.
ABSTRACT Hydrogels are indispensable for the development of next‐generation bioelectronics, soft robotics, and biomedical devices, where their mechanical properties determine performance and reliability. Among strategies to enhance hydrogel mechanics, phase separation enables controlled heterogeneity resulting in gel networks that are reinforced by ...
Yue Shao, Yiming Ma, Baihao Shao, Molly M. Stevens   +3 more
wiley   +1 more source

S. pombe kinesins-8 promote both nucleation and catastrophe of microtubules.

PLoS ONE, 2012
The kinesins-8 were originally thought to be microtubule depolymerases, but are now emerging as more versatile catalysts of microtubule dynamics. We show here that S.
Muriel Erent, Douglas R Drummond, Robert A Cross   +2 more
doaj   +1 more source

CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC

Nature Cell Biology
γ-Tubulin ring complex (γ-TuRC) is the major microtubule-nucleating factor. After nucleation, microtubules can be released from γ-TuRC and stabilized by other proteins, such as CAMSAPs, but the biochemical cross-talk between minus-end regulation pathways
Dipti Rai, Yinlong Song, Shasha Hua, Kelly E. Stecker, Jooske L. Monster, Victor C. Yin, Riccardo Stucchi, Yixin Xu, Yaqian Zhang, Fangrui Chen, E. Katrukha, M. Altelaar, Albert J. R. Heck, Michal Wieczorek, Kai Jiang, A. Akhmanova   +15 more
semanticscholar   +1 more source

A Phase‐Resolved Geometric Deep Learning Framework Maps Structural Determinants of Disease‐Associated Protein Aggregation and Guides Suppressor Design

Advanced Science, EarlyView.
SKALE 2.0 maps disease‐associated protein aggregation as a phase‐resolved structural process, linking mutation‐induced geometric perturbations to nucleation, elongation, and suppressor design. Across neurodegenerative proteins, the framework reveals cryptic aggregation vulnerabilities, separates phase‐concordant and phase‐switching mutations, and ...
Jia Shen Sio, Wei Xuan Wilson Loo, Yan Shan Loo, Wen Xin Tan, Hui Xuan Lim, Huitao Liu, Chen Seng Ng   +6 more
wiley   +1 more source