ArticleMolecular biology of the cell2014
Peptide aptamers define distinct EB1- and EB3-binding motifs and interfere with microtubule dynamics.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- End binding-3 inhibitor activates regenerative program in age-related macular degeneration.Cell reports. Medicine · 2023Article
- SxIP binding disrupts the constitutive homodimer interface of EB1 and stabilizes EB1 monomer.Biophysical journal · 2021Article
- NOD is a plus end-directed motor that binds EB1 via a new microtubule tip localization sequence.The Journal of cell biology · 2018Article
- The HCMV Assembly Compartment Is a Dynamic Golgi-Derived MTOC that Controls Nuclear Rotation and Virus Spread.Developmental cell · 2018Article
- Regulation of end-binding protein EB1 in the control of microtubule dynamics.Cellular and molecular life sciences : CMLS · 2017Review
- Microtubule plus-end tracking proteins in neuronal development.Cellular and molecular life sciences : CMLS · 2016Review
- Control of microtubule organization and dynamics: two ends in the limelight.Nature reviews. Molecular cell biology · 2015Review
- Microtubule-Associated Protein EB3 Regulates IP3 Receptor Clustering and Ca(2+) Signaling in Endothelial Cells.Cell reports · 2015Article
- The microtubule-associated protein EB1 links AIM2 inflammasomes with autophagy-dependent secretion.The Journal of biological chemistry · 2014Article
- Reconstitution of a hierarchical +TIP interaction network controlling microtubule end tracking of dynein.Nature cell biology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
EB1 is a conserved protein that plays a central role in regulating microtubule dynamics and organization. It binds directly to microtubule plus ends and recruits other plus end-localizing proteins. Most EB1-binding proteins contain a Ser-any residue-Ile-Pro (SxIP) motif. Here we describe the isolation of peptide aptamers with optimized versions of this motif by screening for interaction with the Drosophila EB1 protein. The use of small peptide aptamers to competitively inhibit protein interaction and function is becoming increasingly recognized as a powerful technique. We show that SxIP aptamers can bind microtubule plus ends in cells and functionally act to displace interacting proteins by competitive binding. Their expression in developing flies can interfere with microtubules, altering their dynamics. We also identify aptamers binding to human EB1 and EB3, which have sequence requirements similar to but distinct from each other and from Drosophila EB1. This suggests that EB1 paralogues within one species may interact with overlapping but distinct sets of proteins in cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.