Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of a novel EB1 acetylation site important for the regulation of microtubule dynamics and cargo recruitment.

Journal of cellular physiology - 1 Mar 2018

Xie Songbo, Yang Yang, Lin Xiaochen, Zhou Jun, Li Dengwen, Liu Min

Abstract excerpt

Microtubule plus ends undergo highly dynamic modifications to regulate different aspects of cellular activities. Most microtubule plus-end tracking proteins (+TIPs) are recruited to the microtubule ends by the master loading factor, end-binding protein 1 (EB1). These proteins coordinately regulate microtubule dynamics and cellular plasticity. Acetylation is known to modulate EB1 function; however, the molecular...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylation
Share to Autophagy
Share to Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microtubule-Associated Proteins

Share to Microtubules

Share to Protein Interaction Domains and Motifs

Share to Protein Processing, Post-Translational

Share to Proteolysis

Source

Identifiers

PMID: 28777446
DOI: 10.1002/jcp.26133

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a novel EB1 acetylation site important for the regulation of microtubule dynamics and cargo recruitment.PMID 28777446Read ↗

GTP-binding facilitates EB1 recruitment onto microtubules by relieving its auto-inhibition.Semantic proximity Read ↗

Phosphorylation of EB1 regulates the recruitment of CLIP-170 and p150glued to the plus ends of astral microtubules.Semantic proximity Read ↗

Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics.Semantic proximity Read ↗

Microtubule plus-end tracking proteins in neuronal development.Semantic proximity Read ↗

A TIRF microscopy assay to decode how tau regulates EB's tracking at microtubule ends.Semantic proximity Read ↗

A phospho-regulated signal motif determines subcellular localization of α-TAT1 for dynamic microtubule acetylationSemantic proximity Read ↗

Aurora-A phosphorylates Augmin complex component Hice1 protein at an N-terminal serine/threonine cluster to modulate its microtubule binding activity during spindle assembly.Semantic proximity Read ↗

Nuclear-localized subtype of end-binding 1 protein regulates spindle organization in Arabidopsis.Semantic proximity Read ↗

Redox-dependent regulation of end-binding protein 1 activity by glutathionylation.Semantic proximity Read ↗

XMAP215-EB1 interaction is required for proper spindle assembly and chromosome segregation in Xenopus egg extract.Semantic proximity Read ↗

Fission yeast Alp14 is a dose-dependent plus end-tracking microtubule polymerase.Semantic proximity Read ↗

Back to the tubule: microtubule dynamics in Parkinson's disease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.