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Status: Bibliographieeintrag

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Verfasst von:Schulte, Bianca [VerfasserIn]   i
 John, Isabel [VerfasserIn]   i
 Simon, Bernd [VerfasserIn]   i
 Brockmann, Christoph [VerfasserIn]   i
 Oelmeier, Stefan A. [VerfasserIn]   i
 Jahraus, Beate [VerfasserIn]   i
 Kirchgessner, Henning [VerfasserIn]   i
 Riplinger, Selina [VerfasserIn]   i
 Carlomagno, Teresa [VerfasserIn]   i
 Wabnitz, Guido H. [VerfasserIn]   i
 Samstag, Yvonne [VerfasserIn]   i
Titel:A reducing milieu renders cofilin insensitive to phosphatidylinositol 4,5-bisphosphate (PIP2) inhibition
Verf.angabe:Bianca Schulte, Isabel John, Bernd Simon, Christoph Brockmann, Stefan A. Oelmeier, Beate Jahraus, Henning Kirchgessner, Selina Riplinger, Teresa Carlomagno, Guido H. Wabnitz and Yvonne Samstag
Jahr:2013
Umfang:10 S.
Teil:volume:288
 year:2013
 number:41
 pages:29430-29439
 extent:10
Fussnoten:Gesehen am 28.06.2021
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : ASBMB Publications, 1905
Jahr Quelle:2013
Band/Heft Quelle:288(2013), 41, Seite 29430-29439
ISSN Quelle:1083-351X
Abstract:Oxidative stress can lead to T cell hyporesponsiveness. A reducing micromilieu (e.g. provided by dendritic cells) can rescue T cells from such oxidant-induced dysfunction. However, the reducing effects on proteins leading to restored T cell activation remained unknown. One key molecule of T cell activation is the actin-remodeling protein cofilin, which is dephosphorylated on serine 3 upon T cell costimulation and has an essential role in formation of mature immune synapses between T cells and antigen-presenting cells. Cofilin is spatiotemporally regulated; at the plasma membrane, it can be inhibited by phosphatidylinositol 4,5-bisphosphate (PIP2). Here, we show by NMR spectroscopy that a reducing milieu led to structural changes in the cofilin molecule predominantly located on the protein surface. They overlapped with the PIP2- but not actin-binding sites. Accordingly, reduction of cofilin had no effect on F-actin binding and depolymerization and did not influence the cofilin phosphorylation state. However, it did prevent inhibition of cofilin activity through PIP2. Therefore, a reducing milieu may generate an additional pool of active cofilin at the plasma membrane. Consistently, in-flow microscopy revealed increased actin dynamics in the immune synapse of untransformed human T cells under reducing conditions. Altogether, we introduce a novel mechanism of redox regulation: reduction of the actin-remodeling protein cofilin renders it insensitive to PIP2 inhibition, resulting in enhanced actin dynamics.
DOI:doi:10.1074/jbc.M113.479766
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1074/jbc.M113.479766
 Volltext: https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)48764-2
 DOI: https://doi.org/10.1074/jbc.M113.479766
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Actin Depolymerizing Factors
 Actins
 Blotting, Western
 Cell Line, Tumor
 Cell Membrane
 Cells, Cultured
 Cofilin
 Cysteine
 Humans
 Magnetic Resonance Spectroscopy
 Models, Molecular
 Molecular Dynamics Simulation
 Mutation
 Oxidation-Reduction
 Phosphatidylinositol 4,5-Diphosphate
 Phosphatidylinositol Signaling
 Phosphorylation
 Polymerization
 Protein Binding
 Protein Conformation
 Protein Structure, Tertiary
 Redox Regulation
 T Cell
 T-Lymphocytes
K10plus-PPN:1761321447
Verknüpfungen:→ Zeitschrift

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