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Motor-dependent microtubule disassembly driven by tubulin tyrosination

Motor-dependent microtubule disassembly driven by tubulin tyrosination

http://www.wikidata.org/entity/Q37267631

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The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions Microtubule plus-end tracking proteins in neuronal development Neurodegeneration and microtubule dynamics: death by a thousand cuts Extracellular and Intracellular Signaling for Neuronal Polarity Molecular mechanisms of dendrite stability Multiple tubulins: evolutionary aspects and biological implications How morphological constraints affect axonal polarity in mouse neurons Structure and Dynamics of Single-isoform Recombinant Neuronal Human Tubulin Detyrosinated microtubules modulate mechanotransduction in heart and skeletal muscle Single molecule imaging reveals differences in microtubule track selection between Kinesin motors Tubulin tyrosine ligase like 12, a TTLL family member with SET- and TTL-like domains and roles in histone and tubulin modifications and mitosis Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin Structural basis of tubulin tyrosination by tubulin tyrosine ligase Targeting Microtubules for Wound Repair Cacnb4 directly couples electrical activity to gene expression, a process defective in juvenile epilepsy INF2 promotes the formation of detyrosinated microtubules necessary for centrosome reorientation in T cells Microtubule-targeting drugs rescue axonal swellings in cortical neurons from spastin knockout mice.In situ imaging in C. elegans reveals developmental regulation of microtubule dynamics Oxidative stress decreases microtubule growth and stability in ventricular myocytes Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes Microtubules and their role in cellular stress in cancer Genome-wide analysis reveals novel and discrete functions for tubulin carboxy-terminal tails The tubulin code: molecular components, readout mechanisms, and functions Epithelial-to-mesenchymal transition promotes tubulin detyrosination and microtentacles that enhance endothelial engagement Post-translational modifications of microtubules.Cytoskeletal signaling: is memory encoded in microtubule lattices by CaMKII phosphorylation?Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions.Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity.The ADNP derived peptide, NAP modulates the tubulin pool: implication for neurotrophic and neuroprotective activities Effects of kinesin-5 inhibition on dendritic architecture and microtubule organization.Tubulin glycylases are required for primary cilia, control of cell proliferation and tumor development in colon.Rescue of tau-induced synaptic transmission pathology by paclitaxel.Kif4 interacts with EB1 and stabilizes microtubules downstream of Rho-mDia in migrating fibroblasts Post-translational modifications of tubulin: pathways to functional diversity of microtubules.Immune synapse: conductor of orchestrated organelle movement.GSK3-mediated instability of tubulin polymers is responsible for the failure of immature CD4+CD8+ thymocytes to polarize their MTOC in response to TCR stimulation Writing and Reading the Tubulin Code.Compound Library Screening Identified Cardiac Glycoside Digitoxin as an Effective Growth Inhibitor of Gefitinib-Resistant Non-Small Cell Lung Cancer via Downregulation of α-Tubulin and Inhibition of Microtubule Formation.Tubulin perturbation leads to unexpected cell wall modifications and affects stomatal behaviour in Populus Kinesin-13 and tubulin posttranslational modifications regulate microtubule growth in axon regeneration

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P2860

Motor-dependent microtubule disassembly driven by tubulin tyrosination

http://www.wikidata.org/entity/Q37267631

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on June 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Motor-dependent microtubule disassembly driven by tubulin tyrosination

@en

Motor-dependent microtubule disassembly driven by tubulin tyrosination.

@nl

type

label

Motor-dependent microtubule disassembly driven by tubulin tyrosination

@en

Motor-dependent microtubule disassembly driven by tubulin tyrosination.

@nl

prefLabel

Motor-dependent microtubule disassembly driven by tubulin tyrosination

@en

Motor-dependent microtubule disassembly driven by tubulin tyrosination.

@nl

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P1433

Journal of Cell Biology

P1476

Motor-dependent microtubule disassembly driven by tubulin tyrosination

@en

P2093

Annie Andrieux

http://www.w3.org/2001/XMLSchema#string

Ayana T Moore

http://www.w3.org/2001/XMLSchema#string

Didier Job

http://www.w3.org/2001/XMLSchema#string

Frank Kozielski

http://www.w3.org/2001/XMLSchema#string

Jacques Brocard

http://www.w3.org/2001/XMLSchema#string

Laurence Lafanechère

http://www.w3.org/2001/XMLSchema#string

Leticia Peris

http://www.w3.org/2001/XMLSchema#string

Linda Wordeman

http://www.w3.org/2001/XMLSchema#string

Michael Wagenbach

http://www.w3.org/2001/XMLSchema#string

P2860

Aurora B regulates MCAK at the mitotic centromere

Cytoplasmic linker proteins promote microtubule rescue in vivo

MCAK associates with the tips of polymerizing microtubules

The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells.

Plus end-specific depolymerase activity of Kip3, a kinesin-8 protein, explains its role in positioning the yeast mitotic spindle.

Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin

The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends

MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro

Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends.

A vital role of tubulin-tyrosine-ligase for neuronal organization.

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1159-1166

http://www.w3.org/2001/XMLSchema#string

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scholarly article

P356

10.1083/JCB.200902142

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P407

P433

7

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P478

185

http://www.w3.org/2001/XMLSchema#string

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2009-06-01T00:00:00Z

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26328424

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19564401

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2712961

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