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  1. Article ; Online: Phosphoinositide Regulation of TRP Channels: A Functional Overview in the Structural Era.

    Rohacs, Tibor

    Annual review of physiology

    2023  Volume 86, Page(s) 329–355

    Abstract: Transient receptor potential (TRP) ion channels have diverse activation mechanisms including physical stimuli, such as high or low temperatures, and a variety of intracellular signaling molecules. Regulation by phosphoinositides and their derivatives is ... ...

    Abstract Transient receptor potential (TRP) ion channels have diverse activation mechanisms including physical stimuli, such as high or low temperatures, and a variety of intracellular signaling molecules. Regulation by phosphoinositides and their derivatives is their only known common regulatory feature. For most TRP channels, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P
    MeSH term(s) Humans ; Transient Receptor Potential Channels ; Phosphatidylinositols/metabolism ; Cryoelectron Microscopy
    Chemical Substances Transient Receptor Potential Channels ; Phosphatidylinositols
    Language English
    Publishing date 2023-10-23
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207933-1
    ISSN 1545-1585 ; 0066-4278
    ISSN (online) 1545-1585
    ISSN 0066-4278
    DOI 10.1146/annurev-physiol-042022-013956
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  2. Article ; Online: Keeping pain away by distancing the plasma membrane from the endoplasmic reticulum.

    Rohacs, Tibor

    The Journal of physiology

    2021  Volume 599, Issue 7, Page(s) 1941–1942

    MeSH term(s) Cell Membrane ; Endoplasmic Reticulum ; Humans ; Membrane Proteins ; Pain ; Sensory Receptor Cells
    Chemical Substances Membrane Proteins ; junctophilin
    Language English
    Publishing date 2021-03-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 3115-x
    ISSN 1469-7793 ; 0022-3751
    ISSN (online) 1469-7793
    ISSN 0022-3751
    DOI 10.1113/JP281480
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  3. Article ; Online: TMEM120A/TACAN: A putative regulator of ion channels, mechanosensation, and lipid metabolism.

    Gabrielle, Matthew / Rohacs, Tibor

    Channels (Austin, Tex.)

    2023  Volume 17, Issue 1, Page(s) 2237306

    Abstract: TMEM120A (TACAN) is an enigmatic protein with several seemingly unconnected functions. It was proposed to be an ion channel involved in sensing mechanical stimuli, and knockdown/knockout experiments have implicated that TMEM120A may be necessary for ... ...

    Abstract TMEM120A (TACAN) is an enigmatic protein with several seemingly unconnected functions. It was proposed to be an ion channel involved in sensing mechanical stimuli, and knockdown/knockout experiments have implicated that TMEM120A may be necessary for sensing mechanical pain. TMEM120A's ion channel function has subsequently been challenged, as attempts to replicate electrophysiological experiments have largely been unsuccessful. Several cryo-EM structures revealed TMEM120A is structurally homologous to a lipid modifying enzyme called Elongation of Very Long Chain Fatty Acids 7 (ELOVL7). Although TMEM120A's channel function is debated, it still seems to affect mechanosensation by inhibiting PIEZO2 channels and by modifying tactile pain responses in animal models. TMEM120A was also shown to inhibit polycystin-2 (PKD2) channels through direct physical interaction. Additionally, TMEM120A has been implicated in adipocyte regulation and in innate immune response against Zika virus. The way TMEM120A is proposed to alter each of these processes ranges from regulating gene expression, acting as a lipid modifying enzyme, and controlling subcellular localization of other proteins through direct binding. Here, we examine TMEM120A's structure and proposed functions in diverse physiological contexts.
    MeSH term(s) Animals ; Lipid Metabolism ; Ion Channels/metabolism ; Pain/genetics ; Touch/genetics ; Lipids ; Zika Virus/metabolism ; Zika Virus Infection
    Chemical Substances Ion Channels ; Lipids
    Language English
    Publishing date 2023-07-31
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 2262854-X
    ISSN 1933-6969 ; 1933-6969
    ISSN (online) 1933-6969
    ISSN 1933-6969
    DOI 10.1080/19336950.2023.2237306
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Phosphatidic acid is an endogenous negative regulator of PIEZO2 channels and mechanical sensitivity.

    Gabrielle, Matthew / Yudin, Yevgen / Wang, Yujue / Su, Xiaoyang / Rohacs, Tibor

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Mechanosensitive PIEZO2 ion channels play roles in touch, proprioception, and inflammatory pain. Currently, there are no small molecule inhibitors that selectively inhibit PIEZO2 over PIEZO1. The TMEM120A protein was shown to inhibit PIEZO2 while leaving ...

    Abstract Mechanosensitive PIEZO2 ion channels play roles in touch, proprioception, and inflammatory pain. Currently, there are no small molecule inhibitors that selectively inhibit PIEZO2 over PIEZO1. The TMEM120A protein was shown to inhibit PIEZO2 while leaving PIEZO1 unaffected. Here we find that TMEM120A expression elevates cellular levels of phosphatidic acid and lysophosphatidic acid (LPA), aligning with its structural resemblance to lipid-modifying enzymes. Intracellular application of phosphatidic acid or LPA inhibited PIEZO2, but not PIEZO1 activity. Extended extracellular exposure to the non-hydrolyzable phosphatidic acid and LPA analogue carbocyclic phosphatidic acid (ccPA) also inhibited PIEZO2. Optogenetic activation of phospholipase D (PLD), a signaling enzyme that generates phosphatidic acid, inhibited PIEZO2, but not PIEZO1. Conversely, inhibiting PLD led to increased PIEZO2 activity and increased mechanical sensitivity in mice in behavioral experiments. These findings unveil lipid regulators that selectively target PIEZO2 over PIEZO1, and identify the PLD pathway as a regulator of PIEZO2 activity.
    Language English
    Publishing date 2024-03-02
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.01.582964
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The newest TRP channelopathy: Gain of function TRPM3 mutations cause epilepsy and intellectual disability.

    Zhao, Siyuan / Rohacs, Tibor

    Channels (Austin, Tex.)

    2021  Volume 15, Issue 1, Page(s) 386–397

    Abstract: Transient Receptor Potential Melastatin 3 (TRPM3) is a ... ...

    Abstract Transient Receptor Potential Melastatin 3 (TRPM3) is a Ca
    MeSH term(s) Epilepsy ; Gain of Function Mutation ; Ganglia, Spinal ; Intellectual Disability ; Pregnenolone
    Chemical Substances pregnenolone sulfate (04Y4D91RG0) ; Pregnenolone (73R90F7MQ8)
    Language English
    Publishing date 2021-04-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2262854-X
    ISSN 1933-6969 ; 1933-6969
    ISSN (online) 1933-6969
    ISSN 1933-6969
    DOI 10.1080/19336950.2021.1908781
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  6. Article ; Online: Regulation of the cold-sensing TRPM8 channels by phosphoinositides and G

    Liu, Luyu / Rohacs, Tibor

    Channels (Austin, Tex.)

    2020  Volume 14, Issue 1, Page(s) 79–86

    Abstract: The Transient Receptor Potential Melastatin 8 (TRPM8) ion channel is an important sensor of environmental cold temperatures. Cold- and menthol-induced activation of this channel requires the presence of the membrane phospholipid phosphatidylinositol 4,5- ... ...

    Abstract The Transient Receptor Potential Melastatin 8 (TRPM8) ion channel is an important sensor of environmental cold temperatures. Cold- and menthol-induced activation of this channel requires the presence of the membrane phospholipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P
    MeSH term(s) Animals ; Cold Temperature ; Humans ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phosphatidylinositols/metabolism ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; Transient Receptor Potential Channels/metabolism
    Chemical Substances Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols ; TRPM Cation Channels ; TRPM8 protein, human ; Transient Receptor Potential Channels
    Language English
    Publishing date 2020-02-26
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2262854-X
    ISSN 1933-6969 ; 1933-6969
    ISSN (online) 1933-6969
    ISSN 1933-6969
    DOI 10.1080/19336950.2020.1734266
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Phosphoinositide signaling in somatosensory neurons.

    Rohacs, Tibor

    Advances in biological regulation

    2015  Volume 61, Page(s) 2–16

    Abstract: Somatosensory neurons of the dorsal root ganglia (DRG) and trigeminal ganglia (TG) are responsible for detecting thermal and tactile stimuli. They are also the primary neurons mediating pain and itch. A large number of cell surface receptors in these ... ...

    Abstract Somatosensory neurons of the dorsal root ganglia (DRG) and trigeminal ganglia (TG) are responsible for detecting thermal and tactile stimuli. They are also the primary neurons mediating pain and itch. A large number of cell surface receptors in these neurons couple to phospholipase C (PLC) enzymes leading to the hydrolysis of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] and the generation of downstream signaling molecules. These neurons also express many different ion channels, several of which are regulated by phosphoinositides. This review will summarize the knowledge on phosphoinositide signaling in DRG neurons, with special focus on effects on sensory and other ion channels.
    MeSH term(s) Animals ; Calcium/metabolism ; Ganglia, Spinal/cytology ; Ganglia, Spinal/metabolism ; Gene Expression Regulation ; Humans ; Ion Channels/classification ; Ion Channels/genetics ; Ion Channels/metabolism ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Neurons/cytology ; Neurons/metabolism ; Pain Perception/physiology ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Sensory Thresholds/physiology ; Signal Transduction ; Touch Perception/physiology ; Trigeminal Ganglion/cytology ; Trigeminal Ganglion/metabolism ; Type C Phospholipases/genetics ; Type C Phospholipases/metabolism
    Chemical Substances Ion Channels ; Isoenzymes ; Phosphatidylinositol 4,5-Diphosphate ; Type C Phospholipases (EC 3.1.4.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2015-12-19
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2667413-0
    ISSN 2212-4934 ; 2212-4926
    ISSN (online) 2212-4934
    ISSN 2212-4926
    DOI 10.1016/j.jbior.2015.11.012
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  8. Article ; Online: Phosphoinositide regulation of TRPV1 revisited.

    Rohacs, Tibor

    Pflugers Archiv : European journal of physiology

    2015  Volume 467, Issue 9, Page(s) 1851–1869

    Abstract: The heat- and capsaicin-sensitive transient receptor potential vanilloid 1 ion channel (TRPV1) is regulated by plasma membrane phosphoinositides. The effects of these lipids on this channel have been controversial. Recent articles re-ignited the debate ... ...

    Abstract The heat- and capsaicin-sensitive transient receptor potential vanilloid 1 ion channel (TRPV1) is regulated by plasma membrane phosphoinositides. The effects of these lipids on this channel have been controversial. Recent articles re-ignited the debate and also offered resolution to place some of the data in a coherent picture. This review summarizes the literature on this topic and provides a detailed and critical discussion on the experimental evidence for the various effects of phosphatidylinositol 4,5-bisphosphayte [PI(4,5)P2 or PIP2] on TRPV1. We conclude that PI(4,5)P2 and potentially its precursor PI(4)P are positive cofactors for TRPV1, acting via direct interaction with the channel, and their depletion by Ca(2+)-induced activation of phospholipase Cδ isoforms (PLCδ) limits channel activity during capsaicin-induced desensitization. Other negatively charged lipids at higher concentrations can also support channel activity, which may explain some controversies in the literature. PI(4,5)P2 also partially inhibits channel activity in some experimental settings, and relief from this inhibition upon PLCβ activation may contribute to sensitization. The negative effect of PI(4,5)P2 is more controversial and its mechanism is less well understood. Other TRP channels from the TRPV and TRPC families may also undergo similar dual regulation by phosphoinositides, thus the complexity of TRPV1 regulation is not unique to this channel.
    MeSH term(s) Animals ; Humans ; Phosphatidylinositols/metabolism ; TRPV Cation Channels/metabolism
    Chemical Substances Phosphatidylinositols ; TRPV Cation Channels
    Language English
    Publishing date 2015-03-11
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 6380-0
    ISSN 1432-2013 ; 0031-6768
    ISSN (online) 1432-2013
    ISSN 0031-6768
    DOI 10.1007/s00424-015-1695-3
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  9. Article ; Online: Computational and functional studies of the PI(4,5)P

    Zhao, Siyuan / Carnevale, Vincenzo / Gabrielle, Matthew / Gianti, Eleonora / Rohacs, Tibor

    The Journal of biological chemistry

    2022  Volume 298, Issue 11, Page(s) 102547

    Abstract: Transient receptor potential melastatin 3 (TRPM3) is a heat-activated ion channel expressed in peripheral sensory neurons and the central nervous system. TRPM3 activity depends on the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PI(4,5) ... ...

    Abstract Transient receptor potential melastatin 3 (TRPM3) is a heat-activated ion channel expressed in peripheral sensory neurons and the central nervous system. TRPM3 activity depends on the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P
    MeSH term(s) TRPM Cation Channels/metabolism ; Ligands ; Phosphatidylinositols/metabolism ; Binding Sites ; Sensory Receptor Cells/metabolism
    Chemical Substances TRPM Cation Channels ; Ligands ; Phosphatidylinositols
    Language English
    Publishing date 2022-09-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.102547
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  10. Article ; Online: Structural basis of the activation of TRPV5 channels by long-chain acyl-Coenzyme-A.

    Lee, Bo-Hyun / De Jesús Pérez, José J / Moiseenkova-Bell, Vera / Rohacs, Tibor

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 5883

    Abstract: Long-chain acyl-coenzyme A (LC-CoA) is a crucial metabolic intermediate that plays important cellular regulatory roles, including activation and inhibition of ion channels. The structural basis of ion channel regulation by LC-CoA is not known. Transient ... ...

    Abstract Long-chain acyl-coenzyme A (LC-CoA) is a crucial metabolic intermediate that plays important cellular regulatory roles, including activation and inhibition of ion channels. The structural basis of ion channel regulation by LC-CoA is not known. Transient receptor potential vanilloid 5 and 6 (TRPV5 and TRPV6) are epithelial calcium-selective ion channels. Here, we demonstrate that LC-CoA activates TRPV5 and TRPV6 in inside-out patches, and both exogenously supplied and endogenously produced LC-CoA can substitute for the natural ligand phosphatidylinositol 4,5-bisphosphate (PI(4,5)P
    MeSH term(s) Cryoelectron Microscopy ; Acyl Coenzyme A ; Binding Sites ; Calcium Channels ; Cell Cycle
    Chemical Substances Acyl Coenzyme A ; Calcium Channels
    Language English
    Publishing date 2023-09-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-41577-z
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