Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export

Autor: Mitchell A. Moseng, Meinan Lyu, Tanadet Pipatpolkai, Przemyslaw Glaza, Corey C. Emerson, Phoebe L. Stewart, Phillip J. Stansfeld, Edward W. Yu

Publikováno v: mBio, Vol 12, Iss 2 (2021)

The bacterial RND superfamily of efflux pumps mediate resistance to a variety of biocides, including Cu(I) and Ag(I) ions. Here we report four cryo-EM structures of the trimeric CusA pump in the presence of Cu(I). Combined with MD simulations, our da

Externí odkaz: https://doaj.org/article/d5623e1c81b943f792bc80254cdda644

Transition between conformational states of the TREK-1 K2P channel promoted by interaction with PIP

Autor: Adisorn, Panasawatwong, Tanadet, Pipatpolkai, Stephen J, Tucker

Publikováno v: Biophysical journal. 121(12)

Members of the TREK family of two-pore domain potassium channels are highly sensitive to regulation by membrane lipids, including phosphatidylinositol-4,5-bisphosphate (PIP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::256e4dcb811f0121a0fee096612fbff6
https://pubmed.ncbi.nlm.nih.gov/35596528

An outer-pore gate modulates the pharmacology of the TMEM16A channel

Autor: Tanadet Pipatpolkai, Angela J. Russell, Paolo Tammaro, Ria L Dinsdale, Phillip J. Stansfeld, Emilio Agostinelli

Publikováno v: Proc Natl Acad Sci U S A

TMEM16A Ca(2+)-activated chloride channels are involved in multiple cellular functions and are proposed targets for diseases such as hypertension, stroke, and cystic fibrosis. This therapeutic endeavor, however, suffers from paucity of selective and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa8232cc27c9273ec37a67d3bcc99e13
https://doi.org/10.1073/pnas.2023572118

The dynamic interplay of PIP2 and ATP in the regulation of the KATP channel

Autor: Tanadet Pipatpolkai, Samuel G. Usher, Natascia Vedovato, Frances M. Ashcroft, Phillip J. Stansfeld

Publikováno v: Pipatpolkai, T, Usher, S G, Vedovato, N, Ashcroft, F M & Stansfeld, P J 2022, ' The dynamic interplay of PIP 2 and ATP in the regulation of the K ATP channel ', The Journal of Physiology, vol. 600, no. 20, pp. 4503-4519 . https://doi.org/10.1113/JP283345

KEY POINTS: The KATP channel is activated by the binding of phosphoinositol-bisphosphate (PIP2 ) lipids and inactivated by the binding of adenosine triphosphate (ATP). K39 has the potential to bind to both PIP2 and ATP. A mutation to this residue (K3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20f11a334096095b3567a7a9f7373d65
https://doi.org/10.1101/2021.05.06.442933

From Bench to Biomolecular Simulation: Phospholipid Modulation of Potassium Channels

Autor: Daniel Quetschlich, Tanadet Pipatpolkai, Phillip J. Stansfeld

Publikováno v: Journal of Molecular Biology

Graphical abstract
Highlights • Interactions of lipids with K+ channels. • Structural basis of PIP2 binding. • Experimental methods for quantifying PIP2-binding to K+ channels. • Molecular simulation methods for studying PIP2 binding.