Tuning phenylalanine fluorination to assess aromatic contributions to protein function and stability in cells

Autor: Grace D. Galles, Daniel T. Infield, Colin J. Clark, Marcus L. Hemshorn, Shivani Manikandan, Frederico Fazan, Ali Rasouli, Emad Tajkhorshid, Jason D. Galpin, Richard B. Cooley, Ryan A. Mehl, Christopher A. Ahern

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)

Aromatic amino acids in proteins support ligand binding and protein stability. To parse the physiocochemical roles of aromatic interactions, here Galles, Infield and co-authors identify pyrrolysine-based aminoacyl-tRNA synthetases that enable the enc

Externí odkaz: https://doaj.org/article/bf16f9a0529447d48911d7bab7bf37ef

Main-chain mutagenesis reveals intrahelical coupling in an ion channel voltage-sensor

Autor: Daniel T. Infield, Kimberly Matulef, Jason D. Galpin, Kin Lam, Emad Tajkhorshid, Christopher A. Ahern, Francis I. Valiyaveetil

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)

The helical transmembrane segments of membrane proteins play central roles in sensory transduction but the mechanistic basis for their function remains unresolved. Here the authors identify regions in the S4 voltage-sensing segment of Shaker potassiu

Externí odkaz: https://doaj.org/article/5389ce9f78e749c898ea82cd26136909

Divergent Cl- and H+ pathways underlie transport coupling and gating in CLC exchangers and channels

Autor: Lilia Leisle, Yanyan Xu, Eva Fortea, Sangyun Lee, Jason D Galpin, Malvin Vien, Christopher A Ahern, Alessio Accardi, Simon Bernèche

Publikováno v: eLife, Vol 9 (2020)

The CLC family comprises H+-coupled exchangers and Cl- channels, and mutations causing their dysfunction lead to genetic disorders. The CLC exchangers, unlike canonical 'ping-pong' antiporters, simultaneously bind and translocate substrates through p

Externí odkaz: https://doaj.org/article/c9ee0e91e4b94b3f972f512b0980c861

Real-time observation of functional specialization among phosphorylation sites in CFTR

Autor: Daniel T. Infield, Miranda E. Schene, Frederico S. Fazan, Grace D. Galles, Jason D. Galpin, Christopher A. Ahern

Publikováno v: Journal of General Physiology. 155

Phosphoregulation is ubiquitous in biology. Defining the functional roles of individual phosphorylation sites within a multivalent system remains particularly challenging. We have therefore applied a chemical biology approach to light-control the sta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7dbd680bdefffd1fbc253e722acb44b3
https://doi.org/10.1085/jgp.202213216

Role of a conserved ion-binding site tyrosine in ion selectivity of the Na+/K+ pump

Autor: Kerri Spontarelli, Daniel T. Infield, Hang N. Nielsen, Rikke Holm, Victoria C. Young, Jason D. Galpin, Christopher A. Ahern, Bente Vilsen, Pablo Artigas

Publikováno v: Spontarelli, K, Infield, D T, Nielsen, H N, Holm, R, Young, V C, Galpin, J D, Ahern, C A, Vilsen, B & Artigas, P 2022, ' Role of a conserved ion-binding site tyrosine in ion selectivity of the Na + /K + pump ', Journal of General Physiology, vol. 154, no. 7, e202113039 . https://doi.org/10.1085/jgp.202113039
Spontarelli, K, Infield, D T, Nielsen, H N, Holm, R, Young, V C, Galpin, J D, Ahern, C A, Vilsen, B & Artigas, P 2022, ' Role of a conserved ion-binding site tyrosine in ion selectivity of the Na/K pump ', pp. 27 . < https://www.cell.com/biophysj/pdf/S0006-3495(21)03555-4.pdf >

The Na/K pump hydrolyses ATP to export three Na and import two Kacross the plasmalemma. Crystal structures identified three ion-binding siteswithin the pump’s a-subunit. Site-I and site-II bind either Na or K, whilesite-III exclusively binds Na. A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eef491355124e8ee3bbb378878c337a
https://pure.au.dk/portal/da/publications/role-of-a-conserved-ionbinding-site-tyrosine-in-ion-selectivity-of-the-nak-pump(bfb93d49-7234-4b6b-bbca-43b48d5d24fd).html