Functional modulation of a pH-sensitive ion channel by a transporter family

Research output: Contribution to journalConference abstract in journalpeer-review

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Functional modulation of a pH-sensitive ion channel by a transporter family. / Poulsen, Mette H.; Xue, Feng; Maurya, Svetlana R.; Kickinger, Stefanie; Usher, Samuel; Wellendorph, Petrine; Lundby, Alicia; Pless, Stephan A.

In: Biophysical Journal, Vol. 122, No. 3 Suppl. 1, 2023, p. 249a.

Research output: Contribution to journalConference abstract in journalpeer-review

Harvard

Poulsen, MH, Xue, F, Maurya, SR, Kickinger, S, Usher, S, Wellendorph, P, Lundby, A & Pless, SA 2023, 'Functional modulation of a pH-sensitive ion channel by a transporter family', Biophysical Journal, vol. 122, no. 3 Suppl. 1, pp. 249a. https://doi.org/10.1016/j.bpj.2022.11.1448

APA

Poulsen, M. H., Xue, F., Maurya, S. R., Kickinger, S., Usher, S., Wellendorph, P., Lundby, A., & Pless, S. A. (2023). Functional modulation of a pH-sensitive ion channel by a transporter family. Biophysical Journal, 122(3 Suppl. 1), 249a. https://doi.org/10.1016/j.bpj.2022.11.1448

Vancouver

Poulsen MH, Xue F, Maurya SR, Kickinger S, Usher S, Wellendorph P et al. Functional modulation of a pH-sensitive ion channel by a transporter family. Biophysical Journal. 2023;122(3 Suppl. 1):249a. https://doi.org/10.1016/j.bpj.2022.11.1448

Author

Poulsen, Mette H. ; Xue, Feng ; Maurya, Svetlana R. ; Kickinger, Stefanie ; Usher, Samuel ; Wellendorph, Petrine ; Lundby, Alicia ; Pless, Stephan A. / Functional modulation of a pH-sensitive ion channel by a transporter family. In: Biophysical Journal. 2023 ; Vol. 122, No. 3 Suppl. 1. pp. 249a.

Bibtex

@article{05ea7b41518448b9886e90b2be767616,
title = "Functional modulation of a pH-sensitive ion channel by a transporter family",
abstract = "The acid-sensing ion channel 1a (ASIC1a) is a trimeric ligand-gated ion channel. Its activation by protons results in influx of Na+ and, to a lesser extent, Ca2+ before the channel rapidly desensitizes. ASIC1a-mediated currents contribute to normal brain function, including long term potentiation, which is important for learning and memory. However, elevated activity of ASIC1a has been directly implicated in the pathogenesis of numerous disorders, such as ischemic brain injury, cancer, pain and Alzheimer's disease. Recent evidence suggests that during such pathological conditions, association with protein interaction partners can affect ASIC1a activity, thereby contributing to neuronal damage and cell death. Consequently, there is an increasing interest in understanding the regulation of ASIC1a by protein-interaction partners, which remain largely enigmatic. Here, we have used a combination of mass spectrometry, biochemistry and electrophysiology to identify a family of transporters that directly interacts with ASIC1a and regulates its function. Depending on the specific transporter isoform present in the channel-transporter complex, the activation of ASIC1a is either prolonged and potentiated or decreased. We anticipate this work to offer promising starting points for therapeutic targeting of ASIC1a-containing macromolecular complexes in various diseases.",
author = "Poulsen, {Mette H.} and Feng Xue and Maurya, {Svetlana R.} and Stefanie Kickinger and Samuel Usher and Petrine Wellendorph and Alicia Lundby and Pless, {Stephan A.}",
year = "2023",
doi = "10.1016/j.bpj.2022.11.1448",
language = "English",
volume = "122",
pages = "249a",
journal = "Biophysical Society. Annual Meeting. Abstracts",
issn = "0523-6800",
publisher = "Biophysical Society",
number = "3 Suppl. 1",

}

RIS

TY - ABST

T1 - Functional modulation of a pH-sensitive ion channel by a transporter family

AU - Poulsen, Mette H.

AU - Xue, Feng

AU - Maurya, Svetlana R.

AU - Kickinger, Stefanie

AU - Usher, Samuel

AU - Wellendorph, Petrine

AU - Lundby, Alicia

AU - Pless, Stephan A.

PY - 2023

Y1 - 2023

N2 - The acid-sensing ion channel 1a (ASIC1a) is a trimeric ligand-gated ion channel. Its activation by protons results in influx of Na+ and, to a lesser extent, Ca2+ before the channel rapidly desensitizes. ASIC1a-mediated currents contribute to normal brain function, including long term potentiation, which is important for learning and memory. However, elevated activity of ASIC1a has been directly implicated in the pathogenesis of numerous disorders, such as ischemic brain injury, cancer, pain and Alzheimer's disease. Recent evidence suggests that during such pathological conditions, association with protein interaction partners can affect ASIC1a activity, thereby contributing to neuronal damage and cell death. Consequently, there is an increasing interest in understanding the regulation of ASIC1a by protein-interaction partners, which remain largely enigmatic. Here, we have used a combination of mass spectrometry, biochemistry and electrophysiology to identify a family of transporters that directly interacts with ASIC1a and regulates its function. Depending on the specific transporter isoform present in the channel-transporter complex, the activation of ASIC1a is either prolonged and potentiated or decreased. We anticipate this work to offer promising starting points for therapeutic targeting of ASIC1a-containing macromolecular complexes in various diseases.

AB - The acid-sensing ion channel 1a (ASIC1a) is a trimeric ligand-gated ion channel. Its activation by protons results in influx of Na+ and, to a lesser extent, Ca2+ before the channel rapidly desensitizes. ASIC1a-mediated currents contribute to normal brain function, including long term potentiation, which is important for learning and memory. However, elevated activity of ASIC1a has been directly implicated in the pathogenesis of numerous disorders, such as ischemic brain injury, cancer, pain and Alzheimer's disease. Recent evidence suggests that during such pathological conditions, association with protein interaction partners can affect ASIC1a activity, thereby contributing to neuronal damage and cell death. Consequently, there is an increasing interest in understanding the regulation of ASIC1a by protein-interaction partners, which remain largely enigmatic. Here, we have used a combination of mass spectrometry, biochemistry and electrophysiology to identify a family of transporters that directly interacts with ASIC1a and regulates its function. Depending on the specific transporter isoform present in the channel-transporter complex, the activation of ASIC1a is either prolonged and potentiated or decreased. We anticipate this work to offer promising starting points for therapeutic targeting of ASIC1a-containing macromolecular complexes in various diseases.

U2 - 10.1016/j.bpj.2022.11.1448

DO - 10.1016/j.bpj.2022.11.1448

M3 - Conference abstract in journal

C2 - 36783227

AN - SCOPUS:85148099633

VL - 122

SP - 249a

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 3 Suppl. 1

ER -

ID: 337353436