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      Pain or gain?

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      Publication date (Electronic, pub):
      Journal: eLife
      Publisher: eLife Sciences Publications, Ltd
      Keywords: TMEM120, coenzyme A, membrane protein, mechanosensation, ion channel, cryo-EM structure, Human, Mouse

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          Abstract

          The 3D structures of a membrane protein called TMEM120A suggest that it may act as an enzyme in fat metabolism rather than as an ion channel that senses mechanical pain.

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          TACAN Is an Ion Channel Involved in Sensing Mechanical Pain

          Lou Beaulieu-Laroche, Marine Christin, Annmarie Donoghue … (2020)
          Article 0 comments Cited 53 times – based on 0 reviews     Review now
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            Coenzyme A, protein CoAlation and redox regulation in mammalian cells

            Ivan Gout (2018)
            In a diverse family of cellular cofactors, coenzyme A (CoA) has a unique design to function in various biochemical processes. The presence of a highly reactive thiol group and a nucleotide moiety offers a diversity of chemical reactions and regulatory interactions. CoA employs them to activate carbonyl-containing molecules and to produce various thioester derivatives (e.g. acetyl CoA, malonyl CoA and 3-hydroxy-3-methylglutaryl CoA), which have well-established roles in cellular metabolism, production of neurotransmitters and the regulation of gene expression. A novel unconventional function of CoA in redox regulation, involving covalent attachment of this coenzyme to cellular proteins in response to oxidative and metabolic stress, has been recently discovered and termed protein CoAlation (S-thiolation by CoA or CoAthiolation). A diverse range of proteins was found to be CoAlated in mammalian cells and tissues under various experimental conditions. Protein CoAlation alters the molecular mass, charge and activity of modified proteins, and prevents them from irreversible sulfhydryl overoxidation. This review highlights the role of a key metabolic integrator CoA in redox regulation in mammalian cells and provides a perspective of the current status and future directions of the emerging field of protein CoAlation.
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              TMEM120A and B: Nuclear Envelope Transmembrane Proteins Important for Adipocyte Differentiation

              Dzmitry Batrakou, Jose I. de las Heras, Rafal Czapiewski … (2015)
              Recent work indicates that the nuclear envelope is a major signaling node for the cell that can influence tissue differentiation processes. Here we present two nuclear envelope trans-membrane proteins TMEM120A and TMEM120B that are paralogs encoded by the Tmem120A and Tmem120B genes. The TMEM120 proteins are expressed preferentially in fat and both are induced during 3T3-L1 adipocyte differentiation. Knockdown of one or the other protein altered expression of several genes required for adipocyte differentiation, Gata3, Fasn, Glut4, while knockdown of both together additionally affected Pparg and Adipoq. The double knockdown also increased the strength of effects, reducing for example Glut4 levels by 95% compared to control 3T3-L1 cells upon pharmacologically induced differentiation. Accordingly, TMEM120A and B knockdown individually and together impacted on adipocyte differentiation/metabolism as measured by lipid accumulation through binding of Oil Red O and coherent anti-Stokes Raman scattering microscopy (CARS). The nuclear envelope is linked to several lipodystrophies through mutations in lamin A; however, lamin A is widely expressed. Thus it is possible that the TMEM120A and B fat-specific nuclear envelope transmembrane proteins may play a contributory role in the tissue-specific pathology of this disorder or in the wider problem of obesity.
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                Author and article information

                Contributors
                Valeria Kalienkova:
                ORCID: https://orcid.org/0000-0002-4143-6172
                Journal
                Journal ID (nlm-ta): eLife
                Journal ID (iso-abbrev): Elife
                Journal ID (publisher-id): eLife
                Title: eLife
                Publisher: eLife Sciences Publications, Ltd
                ISSN (Electronic): 2050-084X
                Publication date (Electronic, pub): 29 September 2021
                Publication date Collection: 2021
                Volume: 10
                Electronic Location Identifier: e73378
                Affiliations
                [1] University of Groningen Groningen Netherlands
                Author information
                https://orcid.org/0000-0002-4143-6172
                Article
                Publisher ID: 73378
                DOI: 10.7554/eLife.73378
                PMC ID: 8480972
                PubMed ID: 34583807
                SO-VID: 0677ce92-4e59-4cbc-b9b7-160446076a67
                Copyright © © 2021, Kalienkova
                License:

                This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

                History
                Date received : 23 September 2021
                Date accepted : 23 September 2021
                Related
                Categories
                Subject: Insight
                Subject: Neuroscience
                Subject: Structural Biology and Molecular Biophysics
                Subject: Membrane Proteins
                Custom metadata
                Author impact statement The 3D structures of a membrane protein called TMEM120A suggest that it may act as an enzyme in fat metabolism rather than as an ion channel that senses mechanical pain.
                Template 1

                ScienceOpen disciplines: Life sciences
                Keywords: tmem120,coenzyme a,membrane protein,mechanosensation,ion channel,cryo-em structure,human,mouse
                Data availability:
                ScienceOpen disciplines: Life sciences
                Keywords: tmem120, coenzyme a, membrane protein, mechanosensation, ion channel, cryo-em structure, human, mouse

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