Evidence map›Paper›PMID 32886100›Full record

ArticleThe Journal of cell biology2020

Genetically encoded live-cell sensor for tyrosinated microtubules.

Shubham Kesarwani, Prakash Lama, Anchal Chandra, P Purushotam Reddy, A S Jijumon, Satish Bodakuntla, Balaji M Rao, Carsten Janke, Ranabir Das, Minhajuddin Sirajuddin

Abstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Shubham KesarwaniCentre for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Gandhi Krishi Vigyan Kendra Campus, Bangalore, India.
Prakash LamaCentre for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Gandhi Krishi Vigyan Kendra Campus, Bangalore, India.
Anchal ChandraNational Center for Biological Sciences, Tata Institute of Fundamental Research, Gandhi Krishi Vigyan Kendra Campus, Bangalore, India.
P Purushotam ReddyNational Center for Biological Sciences, Tata Institute of Fundamental Research, Gandhi Krishi Vigyan Kendra Campus, Bangalore, India.
A S JijumonInstitut Curie, Paris Sciences et Lettres University, Centre National de la Recherche Scientifique UMR3348, Orsay, France.
Satish BodakuntlaInstitut Curie, Paris Sciences et Lettres University, Centre National de la Recherche Scientifique UMR3348, Orsay, France.
Balaji M RaoDepartment of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC.
Carsten JankeInstitut Curie, Paris Sciences et Lettres University, Centre National de la Recherche Scientifique UMR3348, Orsay, France.
Ranabir DasNational Center for Biological Sciences, Tata Institute of Fundamental Research, Gandhi Krishi Vigyan Kendra Campus, Bangalore, India.
Minhajuddin SirajuddinCentre for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Gandhi Krishi Vigyan Kendra Campus, Bangalore, India.

Funding

DBT-Wellcome Trust India Alliance IA/E/15/1/502339DBT-Wellcome Trust India Alliance IA/I/14/2/501533Wellcome Trust
6 · The paper itself

Abstract

Microtubule cytoskeleton exists in various biochemical forms in different cells due to tubulin posttranslational modifications (PTMs). Tubulin PTMs are known to affect microtubule stability, dynamics, and interaction with MAPs and motors in a specific manner, widely known as tubulin code hypothesis. At present, there exists no tool that can specifically mark tubulin PTMs in living cells, thus severely limiting our understanding of their dynamics and cellular functions. Using a yeast display library, we identified a binder against terminal tyrosine of α-tubulin, a unique PTM site. Extensive characterization validates the robustness and nonperturbing nature of our binder as tyrosination sensor, a live-cell tubulin nanobody specific towards tyrosinated microtubules. Using this sensor, we followed nocodazole-, colchicine-, and vincristine-induced depolymerization events of tyrosinated microtubules in real time and found each distinctly perturbs the microtubule polymer. Together, our work describes a novel tyrosination sensor and its potential applications to study the dynamics of microtubule and their PTM processes in living cells.

Indexed as

ColchicineCytoskeletonHEK293 CellsHumansMicrotubule-Associated ProteinsMicrotubulesNocodazoleProtein Processing, Post-TranslationalTubulinTyrosineVincristineColchicineMicrotubule-Associated ProteinsNocodazoleTubulinTyrosineVincristine

Identifiers

PMID32886100
PMCPMC7659708

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.