Evidence map›Paper›PMID 41594623›Full record

ReviewBiomolecules2026

Emerging Roles of Tubulin Isoforms and Their Post-Translational Modifications in Microtubule-Based Transport and Cellular Functions.

Aishwarya R Nair, Nived Saroj, Ambarish Kunwar

Abstract readReview
In one paragraph

Review in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

3 authors.

Aishwarya R NairDepartment of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.
Nived SarojDepartment of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.
Ambarish KunwarDepartment of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.ORCID 0000-0002-8671-7816

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules are hollow cylindrical polymers made up of tubulin. This heterodimeric protein, tubulin, exists in multiple forms: tubulin isotypes and tubulin isoforms. Distinct α- and β-tubulin genes give rise to tubulin isotypes, which differ in their amino acid sequences and cellular expression patterns. The tubulin post-translational modifications (PTMs) encode regulatory information within the microtubule lattice, modifying its biophysical characteristics and shaping interactions with motor proteins and microtubule-associated proteins. Different tubulin isotype compositions and post-translational modification patterns generate distinct tubulin isoforms. These isoforms are tissue-specific and regulate the functions of microtubules in specialized cells and cellular components such as cilia. Tubulin isoforms control cellular transport, regulate mechanosensitivity and shape the cytoskeleton, impacting the cellular functions and homeostasis. This review discusses the tubulin PTMs, including acetylation, methylation, palmitoylation, polyamination, glutamylation, glycylation, tyrosination, phosphorylation, SUMOylation, and ubiquitination, with emphasis on how isotype diversity and PTM-driven regulation together modulate microtubule behaviour, intracellular transport, and cellular functions.

Indexed as

MicrotubulesProtein Processing, Post-TranslationalTubulinAnimalsHumansProtein IsoformsProtein IsoformsTubulinmicrotubulepost-translational modificationstubulin isoformstubulin isotypes

Identifiers

PMID41594623
PMCPMC12838686

What OpenQuestion holds

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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.