Biography:Elisabeth P. Carpenter

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Elisabeth P. Carpenter
Alma materUniversity of Cambridge
Birkbeck, University of London
Scientific career
InstitutionsUniversity of Oxford
Imperial College London
Diamond Light Source

Elisabeth P. Carpenter is a British structural biologist who is a professor at the Nuffield Department of Medicine in Oxford. She solved the three-dimensional structure of human membrane proteins using X-ray crystallography. Carpenter uses X-ray crystallography to understand the atomic positions within proteins.

Early life and education

Carpenter studied biochemistry at the University of Cambridge from 1981 to 1985.[1] She moved to Birkbeck, University of London for doctoral research from 1985 to 1989, where she studied biochemistry and crystallography.[1][2] After completing her doctorate, Carpenter moved to the National Institute for Health Research, which was based at Imperial College London and solved the structures of proteins involved in DNA repair.[1][2] She also investigated toxoplasmosis and muste movement.[2]

Career

She established the Membrane Protein Laboratory at the Diamond Light Source in 2008.[2][3][4] Subsequently, from 2009 to 2020, she worked at the Structural Genomics Consortium at the University of Oxford[1][2][5] with a focus on human membrane proteins.[6][7]

Research

Carpenter is interested in understanding the structure and function of proteins. She studies proteins embedded within cell membranes.[2] The proteins are large hydrophobic surfaces, and understanding their structure is an important step in unravelling the processes of molecules and signals across cell membranes.[2][8]

Carpenter was the first to describe the structure of the human ABC-transporter ABC10, a mitrochonridal protein that is important in the production of heme.[9][10][11] She has studied premature ageing syndromes that are caused by failure of the lamin proteins, and the role of the metalloprotease ZMPSTE24.[12][13][14][15] She has also studied human two-pore potassium channels (K2Ps), protein that gives rise to the background leak current that contributes to membrane potential.[16][17][18][19]

Selected publications

References

  1. ↑ 1.0 1.1 1.2 1.3 "Elisabeth Paula Carpenter". https://orcid.org/0000-0001-9138-2937. 
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 "Carpenter" (in en). 2019-04-25. https://www.thesgc.org/profile/oxford/lcarpenter. 
  3. ↑ "New UK laboratory to focus on important medical targets - - Diamond Light Source". https://www.diamond.ac.uk/Home/News/LatestNews/01_09_08.html. 
  4. ↑ Barford, David; Blundell, Thomas L. (June 2022). "Dame Louise Napier Johnson. 26 September 1940—25 September 2012". Biographical Memoirs of Fellows of the Royal Society 72: 221–250. doi:10.1098/rsbm.2021.0038. 
  5. ↑ Hendrickson, Wayne A (June 2016). "Atomic-level analysis of membrane-protein structure". Nature Structural & Molecular Biology 23 (6): 464–467. doi:10.1038/nsmb.3215. PMID 27273628. 
  6. ↑ Carpenter, Liz. "The High-throughtput Membrane Protein Structural Biology Pipeline at the SGC". https://journals.iucr.org/a/issues/2010/a1/00/a46070/a46070.pdf. 
  7. ↑ Tampé, Robert (1 September 2015). "Membrane Transport and Communication in Frankfurt: Speakers' Summary – Highlights". Biological Chemistry 396 (9–10): 949–954. doi:10.1515/hsz-2015-0211. PMID 26352202. 
  8. ↑ "Liz Carpenter" (in en). https://www.medsci.ox.ac.uk/study/graduateschool/supervisors/liz-carpenter. 
  9. ↑ Qiu, Wei; Liesa, Marc; Carpenter, Elizabeth P.; Shirihai, Orian S. (8 June 2015). "ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione". PLOS ONE 10 (6). doi:10.1371/journal.pone.0129772. PMID 26053025. Bibcode: 2015PLoSO..1029772Q. 
  10. ↑ Shum, Michael; Shintre, Chitra A.; Althoff, Thorsten; Gutierrez, Vincent; Segawa, Mayuko; Saxberg, Alexandra D.; Martinez, Melissa; Adamson, Roslin et al. (19 May 2021). "ABCB10 exports mitochondrial biliverdin, driving metabolic maladaptation in obesity". Science Translational Medicine 13 (594). doi:10.1126/scitranslmed.abd1869. PMID 34011630. 
  11. ↑ Shintre, Chitra A.; Pike, Ashley C. W.; Li, Qiuhong; Kim, Jung-In; Barr, Alastair J.; Goubin, Solenne; Shrestha, Leela; Yang, Jing et al. (11 June 2013). "Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states". Proceedings of the National Academy of Sciences 110 (24): 9710–9715. doi:10.1073/pnas.1217042110. PMID 23716676. Bibcode: 2013PNAS..110.9710S. 
  12. ↑ Spear, Eric D.; Hsu, Erh-Ting; Nie, Laiyin; Carpenter, Elisabeth P.; Hrycyna, Christine A.; Michaelis, Susan (1 July 2018). "ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and/or protein stability". Disease Models & Mechanisms 11 (7). doi:10.1242/dmm.033670. PMID 29794150. 
  13. ↑ Mehmood, Shahid; Marcoux, Julien; Gault, Joseph; Quigley, Andrew; Michaelis, Susan; Young, Stephen G.; Carpenter, Elisabeth P.; Robinson, Carol V. (December 2016). "Mass spectrometry captures off-target drug binding and provides mechanistic insights into the human metalloprotease ZMPSTE24". Nature Chemistry 8 (12): 1152–1158. doi:10.1038/nchem.2591. PMID 27874871. Bibcode: 2016NatCh...8.1152M. 
  14. ↑ Babatz, Timothy D.; Spear, Eric D.; Xu, Wenxin; Sun, Olivia L.; Nie, Laiyin; Carpenter, Elisabeth P.; Michaelis, Susan (January 2021). "Site specificity determinants for prelamin A cleavage by the zinc metalloprotease ZMPSTE24". Journal of Biological Chemistry 296. doi:10.1074/jbc.RA120.015792. PMID 33293369. 
  15. ↑ Quigley, Andrew; Dong, Yin Yao; Pike, Ashley C. W.; Dong, Liang; Shrestha, Leela; Berridge, Georgina; Stansfeld, Phillip J.; Sansom, Mark S. P. et al. (29 March 2013). "The Structural Basis of ZMPSTE24-Dependent Laminopathies". Science 339 (6127): 1604–1607. doi:10.1126/science.1231513. PMID 23539603. Bibcode: 2013Sci...339.1604Q. 
  16. ↑ Rödström, Karin E. J.; Kiper, Aytuğ K.; Zhang, Wei; Rinné, Susanne; Pike, Ashley C. W.; Goldstein, Matthias; Conrad, Linus J.; Delbeck, Martina et al. (18 June 2020). "A lower X-gate in TASK channels traps inhibitors within the vestibule". Nature 582 (7812): 443–447. doi:10.1038/s41586-020-2250-8. PMID 32499642. Bibcode: 2020Natur.582..443R. 
  17. ↑ McClenaghan, Conor; Schewe, Marcus; Aryal, Prafulla; Carpenter, Elisabeth P.; Baukrowitz, Thomas; Tucker, Stephen J. (1 June 2016). "Polymodal activation of the TREK-2 K2P channel produces structurally distinct open states". Journal of General Physiology 147 (6): 497–505. doi:10.1085/jgp.201611601. PMID 27241700. 
  18. ↑ Rödström, Karin E. J.; Cloake, Alexander; Sörmann, Janina; Baronina, Agnese; Smith, Kathryn H. M.; Pike, Ashley C. W.; Ang, Jackie; Proks, Peter et al. (16 May 2024). "Extracellular modulation of TREK-2 activity with nanobodies provides insight into the mechanisms of K2P channel regulation". Nature Communications 15 (1). doi:10.1038/s41467-024-48536-2. PMID 38755204. Bibcode: 2024NatCo..15.4173R. 
  19. ↑ Dong, Yin Yao; Pike, Ashley C. W.; Mackenzie, Alexandra; McClenaghan, Conor; Aryal, Prafulla; Dong, Liang; Quigley, Andrew; Grieben, Mariana et al. (13 March 2015). "K2P channel gating mechanisms revealed by structures of TREK-2 and a complex with Prozac". Science 347 (6227): 1256–1259. doi:10.1126/science.1261512. PMID 25766236. Bibcode: 2015Sci...347.1256D. 



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