LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 93

Search options

  1. Article: Myristoylated Neuronal Calcium Sensor-1 captures the ciliary vesicle at distal appendages.

    Kanie, Tomoharu / Ng, Roy / Abbott, Keene L / Pongs, Olaf / Jackson, Peter K

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The primary cilium is a microtubule-based organelle that cycles through assembly and disassembly. In many cell types, formation of the cilium is initiated by recruitment of ciliary vesicles to the distal appendage of the mother centriole. However, the ... ...

    Abstract The primary cilium is a microtubule-based organelle that cycles through assembly and disassembly. In many cell types, formation of the cilium is initiated by recruitment of ciliary vesicles to the distal appendage of the mother centriole. However, the distal appendage mechanism that directly captures ciliary vesicles is yet to be identified. In an accompanying paper, we show that the distal appendage protein, CEP89, is important for thef ciliary vesicle recruitment, but not for other steps of cilium formation (Tomoharu Kanie, Love, Fisher, Gustavsson, & Jackson, 2023). The lack of a membrane binding motif in CEP89 suggests that it may indirectly recruit ciliary vesicles via another binding partner. Here, we identify Neuronal Calcium Sensor-1 (NCS1) as a stoichiometric interactor of CEP89. NCS1 localizes to the position between CEP89 and a ciliary vesicle marker, RAB34, at the distal appendage. This localization was completely abolished in CEP89 knockouts, suggesting that CEP89 recruits NCS1 to the distal appendage. Similarly to CEP89 knockouts, ciliary vesicle recruitment as well as subsequent cilium formation was perturbed in NCS1 knockout cells. The ability of NCS1 to recruit the ciliary vesicle is dependent on its myristoylation motif and NCS1 knockout cells expressing myristoylation defective mutant failed to rescue the vesicle recruitment defect despite localizing proper localization to the centriole. In sum, our analysis reveals the first known mechanism for how the distal appendage recruits the ciliary vesicles.
    Language English
    Publishing date 2023-01-10
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.01.06.523037
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article: NCS-1 Deficiency Is Associated With Obesity and Diabetes Type 2 in Mice.

    Ratai, Olga / Hermainski, Joanna / Ravichandran, Keerthana / Pongs, Olaf

    Frontiers in molecular neuroscience

    2019  Volume 12, Page(s) 78

    Abstract: Neuronal calcium sensor-1 (NCS-1) knockout (KO) in mice (NCS- ... ...

    Abstract Neuronal calcium sensor-1 (NCS-1) knockout (KO) in mice (NCS-1
    Language English
    Publishing date 2019-04-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2019.00078
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: TREKing noxious thermosensation.

    Pongs, Olaf

    The EMBO journal

    2009  Volume 28, Issue 9, Page(s) 1195–1196

    MeSH term(s) Animals ; Electrophysiology ; Hot Temperature ; Mice ; Mice, Inbred C57BL ; Pain ; Potassium Channels/genetics ; Potassium Channels/physiology ; Potassium Channels, Tandem Pore Domain/genetics ; Potassium Channels, Tandem Pore Domain/physiology ; Sensory Receptor Cells/cytology ; Sensory Receptor Cells/metabolism ; Thermosensing/genetics ; Thermosensing/physiology
    Chemical Substances Kcnk4 protein, mouse ; Potassium Channels ; Potassium Channels, Tandem Pore Domain ; potassium channel protein TREK-1
    Language English
    Publishing date 2009-05-04
    Publishing country England
    Document type Comment ; Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/emboj.2009.107
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article: Ins and outs of cardiac voltage-gated potassium channels.

    Pongs, Olaf

    Current opinion in pharmacology

    2009  Volume 9, Issue 3, Page(s) 311–315

    Abstract: Voltage-gated potassium (Kv) channels play an important role in regulating cardiac muscle excitability by controlling action potential duration and frequency. Essential for this activity is proper localization and organization of the cardiac Kv channels ... ...

    Abstract Voltage-gated potassium (Kv) channels play an important role in regulating cardiac muscle excitability by controlling action potential duration and frequency. Essential for this activity is proper localization and organization of the cardiac Kv channels in specific microdomains of the plasma membrane. The underlying processes involve tight control of anterograde and retrograde Kv channel trafficking into and out of the plasma membrane. Thus, cardiac Kv channel density at the cell surface is regulated by a dynamic interplay of endocytotic and recycling pathways, the mechanisms of which are mostly unknown. Recent studies have indicated that the lipid composition in the Kv channel surround profoundly influences these processes. Local differences in lipid composition altering the mechanic state of the lipid bilayer or a specific interaction with an important domain of the Kv channel markedly affect voltage-sensitive gating, clustering, and mobility of cardiac Kv channels and, thereby, the excitability in the healthy and diseased heart muscles.
    MeSH term(s) Animals ; Cell Membrane/metabolism ; Endocytosis ; Humans ; Lipids/chemistry ; Myocardium/metabolism ; Myocytes, Cardiac/metabolism ; Potassium Channels, Voltage-Gated/metabolism ; Protein Transport
    Chemical Substances Lipids ; Potassium Channels, Voltage-Gated
    Language English
    Publishing date 2009-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2037057-X
    ISSN 1471-4973 ; 1471-4892
    ISSN (online) 1471-4973
    ISSN 1471-4892
    DOI 10.1016/j.coph.2009.03.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article ; Conference proceedings: Ion Channel Target--Informa conference.

    Pongs, Olaf

    IDrugs : the investigational drugs journal

    2008  Volume 11, Issue 5, Page(s) 318–321

    MeSH term(s) Analgesics/adverse effects ; Analgesics/pharmacology ; Animals ; Biomedical Research ; Calcium Channels/drug effects ; Cardiovascular Diseases/chemically induced ; Humans ; Ion Channels/drug effects ; Ion Channels/genetics ; Ion Channels/metabolism ; Membrane Transport Modulators/adverse effects ; Membrane Transport Modulators/pharmacology ; Mice ; Mice, Knockout ; Nerve Tissue Proteins/drug effects ; Potassium Channels, Tandem Pore Domain/drug effects ; Receptors, Nicotinic/drug effects ; Receptors, Purinergic P2/drug effects ; Receptors, Purinergic P2X ; TRPA1 Cation Channel ; TRPM Cation Channels/drug effects ; TRPV Cation Channels/drug effects ; Transient Receptor Potential Channels/drug effects
    Chemical Substances Analgesics ; Calcium Channels ; Ion Channels ; Membrane Transport Modulators ; Nerve Tissue Proteins ; Potassium Channels, Tandem Pore Domain ; Receptors, Nicotinic ; Receptors, Purinergic P2 ; Receptors, Purinergic P2X ; TRPA1 Cation Channel ; TRPA1 protein, human ; TRPM Cation Channels ; TRPM4 protein, mouse ; TRPV Cation Channels ; Transient Receptor Potential Channels ; potassium channel protein TREK-1
    Language English
    Publishing date 2008-05
    Publishing country England
    Document type Congresses
    ZDB-ID 2086568-5
    ISSN 2040-3410 ; 1369-7056
    ISSN (online) 2040-3410
    ISSN 1369-7056
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  6. Article ; Online: Editorial overview: Cardiovascular and renal: Novel therapeutic strategies and approaches for targeting unmet cardiovascular needs.

    Kaczorowski, Gregory J / Pongs, Olaf

    Current opinion in pharmacology

    2014  Volume 15, Page(s) v–viii

    MeSH term(s) Animals ; Cardiovascular Diseases/drug therapy ; Cardiovascular Diseases/metabolism ; Cardiovascular System/metabolism ; Humans ; Ion Channels/metabolism ; Kidney/metabolism ; Kidney Diseases/drug therapy ; Kidney Diseases/metabolism ; Molecular Targeted Therapy
    Chemical Substances Ion Channels
    Language English
    Publishing date 2014-04
    Publishing country England
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 2037057-X
    ISSN 1471-4973 ; 1471-4892
    ISSN (online) 1471-4973
    ISSN 1471-4892
    DOI 10.1016/j.coph.2014.02.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  7. Article ; Online: TRPM4 channels in the cardiovascular system.

    Kruse, Martin / Pongs, Olaf

    Current opinion in pharmacology

    2013  Volume 15, Page(s) 68–73

    Abstract: The non-selective Transient Receptor Potential Melastatin 4 (TRPM4) cation channel is abundantly expressed in cardiac cells, being involved in several aspects of cardiac rhythmicity, including cardiac conduction, pace making and action-potential ... ...

    Abstract The non-selective Transient Receptor Potential Melastatin 4 (TRPM4) cation channel is abundantly expressed in cardiac cells, being involved in several aspects of cardiac rhythmicity, including cardiac conduction, pace making and action-potential repolarization. Dominantly inherited mutations in the TRPM4 gene are associated with the cardiac bundle-branch disorder progressive familial heart block type I (PFHBI) and isolated cardiac conduction disease (ICCD) giving rise to atrio-ventricular conduction block (AVB), right bundle branch block, bradycardia, and the Brugada syndrome. The mutant phenotypes closely resemble those associated with mutations in the SCN5A gene, encoding the voltage-gated Na(+) channel NaV1.5. These observations and the unexpected partnership with sulfonylurea-receptors (SURs) makes the TRPM4 channel a promising novel target for treatment of cardiac disorders.
    MeSH term(s) Animals ; Cardiovascular Physiological Phenomena ; Cardiovascular System/metabolism ; Humans ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; TRPM Cation Channels/physiology
    Chemical Substances TRPM Cation Channels
    Language English
    Publishing date 2013-12-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2037057-X
    ISSN 1471-4973 ; 1471-4892
    ISSN (online) 1471-4973
    ISSN 1471-4892
    DOI 10.1016/j.coph.2013.12.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  8. Article: NCS-1 Deficiency Affects mRNA Levels of Genes Involved in Regulation of ATP Synthesis and Mitochondrial Stress in Highly Vulnerable

    Simons, Carsten / Benkert, Julia / Deuter, Nora / Poetschke, Christina / Pongs, Olaf / Schneider, Toni / Duda, Johanna / Liss, Birgit

    Frontiers in molecular neuroscience

    2019  Volume 12, Page(s) 252

    Abstract: ... Neuronal ... ...

    Abstract Neuronal Ca
    Language English
    Publishing date 2019-11-27
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2019.00252
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  9. Article ; Online: Coupling of voltage-sensors to the channel pore: a comparative view.

    Vardanyan, Vitya / Pongs, Olaf

    Frontiers in pharmacology

    2012  Volume 3, Page(s) 145

    Abstract: The activation of voltage-dependent ion channels is initiated by potential-induced conformational rearrangements in the voltage-sensor domains that propagates to the pore domain (PD) and finally opens the ion conduction pathway. In potassium channels ... ...

    Abstract The activation of voltage-dependent ion channels is initiated by potential-induced conformational rearrangements in the voltage-sensor domains that propagates to the pore domain (PD) and finally opens the ion conduction pathway. In potassium channels voltage-sensors are covalently linked to the pore via S4-S5 linkers at the cytoplasmic site of the PD. Transformation of membrane electric energy into the mechanical work required for the opening or closing of the channel pore is achieved through an electromechanical coupling mechanism, which involves local interaction between residues in S4-S5 linker and pore-forming alpha helices. In this review we discuss present knowledge and open questions related to the electromechanical coupling mechanism in most intensively studied voltage-gated Shaker potassium channel and compare structure-functional aspects of coupling with those observed in distantly related ion channels. We focus particularly on the role of electromechanical coupling in modulation of the constitutive conductance of ion channels.
    Language English
    Publishing date 2012-07-27
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587355-6
    ISSN 1663-9812 ; 1663-9812
    ISSN (online) 1663-9812
    ISSN 1663-9812
    DOI 10.3389/fphar.2012.00145
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  10. Article ; Online: Probing Conformational Changes during the Gating Cycle of a Potassium Channel in Lipid Bilayers.

    van der Cruijsen, Elwin A W / Prokofyev, Alexander V / Pongs, Olaf / Baldus, Marc

    Biophysical journal

    2017  Volume 112, Issue 1, Page(s) 99–108

    Abstract: Ion conduction across the cellular membrane requires the simultaneous opening of activation and inactivation gates of the ... ...

    Abstract Ion conduction across the cellular membrane requires the simultaneous opening of activation and inactivation gates of the K
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Cardiolipins/metabolism ; Cell Membrane/metabolism ; Ion Channel Gating ; Lipid Bilayers/metabolism ; Models, Molecular ; Potassium Channels/chemistry ; Potassium Channels/metabolism ; Protein Conformation
    Chemical Substances Bacterial Proteins ; Cardiolipins ; Lipid Bilayers ; Potassium Channels
    Language English
    Publishing date 2017-01-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2016.12.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top