ReviewPflugers Archiv : European journal of physiology2016
The mucolipin-2 (TRPML2) ion channel: a tissue-specific protein crucial to normal cell function.
Review in Pflugers Archiv : European journal of physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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.
Who cites it
28 citing papers in PubMed, 56 citations in OpenAlex.
- Calcium and TRPML-Mediated Autophagy: Implications in Cancer, Cardiovascular Diseases, and Cardio-Oncology.Cardiovascular toxicology · 2026Review
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Transient receptor potential channels in viral infectious diseases: Biological characteristics and regulatory mechanisms.Journal of advanced research · 2025Review
- Lysosomal ion channels and pain.Pain reports · 2025Review
- The Unique Roles of Ion Channels in Pluripotent Stem Cells in Response to Biological Stimuli.Biology · 2024Review
- Pathological Functions of Lysosomal Ion Channels in the Central Nervous System.International journal of molecular sciences · 2024Review
- Endolysosomal TRPML1 channel regulates cancer cell migration by altering intracellular trafficking of E-cadherin and βThe Journal of biological chemistry · 2024Article
- TRP Channels in Cancer: Signaling Mechanisms and Translational Approaches.Biomolecules · 2023Review
- TRPML2 Mucolipin Channels Drive the Response of Glioma Stem Cells to Temozolomide and Affect the Overall Survival in Glioblastoma Patients.International journal of molecular sciences · 2022Article
- Article
- Probing predilection to Crohn's disease and Crohn's disease flares: A crowd-sourced bioinformatics approach.Journal of pathology informatics · 2022Article
- Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein ofInsects · 2021Article
- Endolysosomal TRPMLs in Cancer.Biomolecules · 2021Review
- TRPML2 is an osmo/mechanosensitive cation channel in endolysosomal organelles.Science advances · 2020Article
- Neuropathophysiology, Genetic Profile, and Clinical Manifestation of Mucolipidosis IV-A Review and Case Series.International journal of molecular sciences · 2020Review
- Review
- TRP Channels as Interior Designers: Remodeling the Endolysosomal Compartment in Natural Killer Cells.Frontiers in immunology · 2020Review
- Emerging Role of Mucolipins TRPML Channels in Cancer.Frontiers in oncology · 2020Article
- Involvement of the TRPML Mucolipin Channels in Viral Infections and Anti-viral Innate Immune Responses.Frontiers in immunology · 2020Review
- Calcium signalling in T cells.Nature reviews. Immunology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The discovery of the TRPML subfamily of ion channels has created an exciting niche in the fields of membrane trafficking, signal transduction, autophagy, and metal homeostasis. The TRPML protein subfamily consists of three members, TRPML1, TRPML2, and TRPML3, which are encoded by MCOLN1, MCOLN2, and MCOLN3 genes, respectively. They are non-selective cation channels with six predicted transmembrane domains and intracellular amino- and carboxyl-terminus regions. They localize to the plasma membrane, endosomes, and lysosomes of cells. TRPML1 is associated with the human lysosomal storage disease known as mucolipidosis type IV (MLIV), but TRPML2 and TRPML3 have not been linked with a human disease. Although TRPML1 is expressed in many tissues, TRPML3 is expressed in a varied but limited set of tissues, while TRPML2 has a more limited expression pattern where it is mostly detected in lymphoid and myeloid tissues. This review focuses on TRPML2 because it appears to play an important, yet unrecognized role in the immune system. While the evidence has been mostly indirect, we present and discuss relevant data that strengthen the connection of TRPML2 with cellular immunity. We also discuss the functional redundancy between the TRPML proteins, and how such features could be exploited as a potential therapeutic strategy for MLIV disease. We present evidence that TRPML2 expression may complement certain phenotypic alterations in MLIV cells and briefly examine the challenges of functional complementation. In conclusion, the function of TRPML2 still remains obscure, but emerging data show that it may serve a critical role in immune cell development and inflammatory responses.
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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.