Evidence map›Paper›PMID 40317801›Full record

ReviewJournal of neuroscience research2025

Tubulin Polymerization Promoting Proteins: Functional Diversity With Implications in Neurological Disorders.

Paloma J Diaz, Qian Shi, Priscilla Y McNeish, Swati Banerjee

Abstract readReview
In one paragraph

Review in Journal of neuroscience research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Experience-mediated transcriptional memory correlates with hypoxia resistance in the nervous system of the sea hareAmerican journal of physiology. Regulatory, integrative and comparative physiology · 2025
    Article
  3. Article
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

4 authors.

Paloma J DiazDepartment of Cellular and Integrative Physiology, University of Texas Health Science Center San Antonio, Joe R. and Teresa Lozano Long School of Medicine, San Antonio, Texas, USA.ORCID 0009-0001-5819-3373
Qian ShiDepartment of Cellular and Integrative Physiology, University of Texas Health Science Center San Antonio, Joe R. and Teresa Lozano Long School of Medicine, San Antonio, Texas, USA.
Priscilla Y McNeishDepartment of Cellular and Integrative Physiology, University of Texas Health Science Center San Antonio, Joe R. and Teresa Lozano Long School of Medicine, San Antonio, Texas, USA.
Swati BanerjeeDepartment of Cellular and Integrative Physiology, University of Texas Health Science Center San Antonio, Joe R. and Teresa Lozano Long School of Medicine, San Antonio, Texas, USA.ORCID 0000-0001-8749-5197

Funding

Institute for Integration of Medicine & Science: A Partnership to Improve HealthUM1TR004538 · NCATS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI ROBERT A CLARK, Kenneth M Hargreaves · 2023 to 2026
$22.3M
Molecular Mechanisms of Tubulin Polymerization Promoting Protein in Mitochondrial Function and Neuronal SurvivalR01NS134867 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Swati Banerjee · 2024 to 2026
$1.2M
Summer Physiology Undergraduate Researcher (SPUR) ProgramR25NS115552 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Swati Banerjee · 2021 to 2026
$673k
Developing a Drosophila Model of Parkinson’s DiseaseR03NS116308 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BANERJEE, SWATI · 2020 to 2021
$196k
Institute for Integration of Medicine and ScienceLong School of Medicine, UT Health San AntonioNCATS NIH HHS UM1 TR004538NINDS NIH HHS R01 NS134867NINDS NIH HHS R03 NS116308NINDS NIH HHS R25 NS115552Office of Extramural Research, National Institutes of Health R01NS134867Office of Extramural Research, National Institutes of Health R03NS116308Office of Extramural Research, National Institutes of Health R25NS115552
6 · The paper itself

Abstract

Tubulin Polymerization Promoting Proteins (TPPPs) are highly conserved across species but remain poorly understood. There are three TPPP genes in humans, with only one homologous TPPP gene in invertebrates, such as Drosophila and C. elegans. The human TPPP (TPPP1/p25/p25α) is enriched in the brain and shares sequence similarities with the invertebrate TPPPs. TPPP/p25 associates with microtubules and plays a pivotal role in microtubule dynamics, bundling, and polymerization, thereby stabilizing the microtubular network. This is essential for cytoskeletal organization and proper functioning of neurons and glial cells, including axonal growth, regeneration, migration, trafficking, synapse formation, and myelination of axons. However, studies have also uncovered that besides its cytoplasmic/microtubular localization, TPPP/p25 is present in other subcellular compartments, including the mitochondria and nucleus, underscoring the presence of additional novel functions. At the molecular level, TPPP/p25 is predicted to exist as an intrinsically disordered protein and is implicated in neurological and neurodegenerative disorders, including Parkinson's and related disorders and Multiple Sclerosis. In this article, we provide a comprehensive overview of TPPP/p25, highlighting its evolutionary conservation, cellular and subcellular localization, established and emerging functions in the nervous system, interacting partners, potential clinical relevance to human neurological disorders, and conclude with unresolved questions and future areas of study.

Indexed as

Nerve Tissue ProteinsNervous System DiseasesTubulinAnimalsHumansMicrotubulesPolymerizationNerve Tissue ProteinsTPPP protein, humanTubulinCNSensheathmentmicrotubulemitochondriaα‐synucleinopathies

Identifiers

PMID40317801
PMCPMC12047068

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.