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Franz-Ulrich Hartl

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Franz-Ulrich Hartl (born 10 March 1957) is a German biochemist and the current Executive Director of the Max Planck Institute of Biochemistry. He is known for his pioneering work in chaperone-mediated protein folding.

Franz-Ulrich Hartl
Born (1957-03-10) 10 March 1957 (age 67)[2]
Essen, West Germany[2]
Alma materHeidelberg University
Ludwig Maximilian University of Munich
Known forResearch of protein folding
AwardsGottfried Wilhelm Leibniz Prize
Gairdner Foundation International Award
Wiley Prize in Biomedical Science
Order of Merit of the Federal Republic of Germany
Heinrich Wieland Prize
Albert Lasker Award for Basic Medical Research
Shaw Prize
Albany Medical Center Prize
E.B. Wilson Medal
Breakthrough Prize in Life Sciences
Bavarian Maximilian Order for Science and Art
Schleiden Medal[1]
Scientific career
FieldsBiochemistry
InstitutionsMax Planck Institute of Biochemistry
Howard Hughes Medical Institute
Cornell University
Memorial Sloan Kettering Cancer Center
University of California, Los Angeles[1]
ThesisDie Steuerung peroxisomaler Enzymaktivitäten durch Schilddrüsenhormon in der Leber der Ratte (The Regulation of Rat Liver Peroxisomal Metabolism by Thyroid Hormones) (1985)

Early life and education

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Hartl was born in Essen, West Germany in 1957 to an electrical engineer father and a home economics teacher mother. His family moved to a village in northern part of the Black Forest when he was four. He was intrigued with biology since a young age, thanks to his hobby microscopist grandfather and a family friend who was a biology teacher.[2] Hartl specifically became interested in biochemistry in high school after reading James Watson's account of the discovery of the helical structure of DNA, prompting him to study medicine and specialise in biochemistry at Heidelberg University.[2][3] It was during this period when he had his first research experience, studying peroxisomes in rat liver. Hartl completed his MD degree in 1985.[1]

Career

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After receiving his MD degree, one of the external examiners of Hartl's thesis, Walter Neupert, invited him to join his group at the Institute of Physiological Chemistry of the Ludwig Maximilian University of Munich as a postdoctoral researcher.[2] Hartl then achieved habilitation in 1990,[1] which is one of the requirements for professorship in Germany.[4][5]

In 1989, Hartl spent a year as a postdoctoral fellow at William T. Wickner's group at the University of California, Los Angeles. In 1991, after obtaining habilitation, he moved to the Cellular Biochemistry and Biophysics Program of the Memorial Sloan Kettering Cancer Center, also becoming an associate professor at the Cornell University Medical College (now Weill Cornell Medicine). He was promoted to full professor 3 years later.[1]

Hartl returned to Germany in 1997 to become one of the Directors of the Max Planck Institute of Biochemistry (MPIB).[1] The Executive Director of MPIB rotates among the Directors every year, and Hartl is the current Executive Director for the year 2023.[6][7]

During his time at the Memorial Sloan Kettering Cancer Center, Hartl was a William E. Snee Chair and a Howard Hughes Medical Institute investigator (1994-1997).[8]

Research

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Hartl was known for his discovery of chaperone-mediated protein folding, made together with Arthur L. Horwich. Protein folding is the process where proteins attain their three-dimensional shapes required to be functional.[9] His research on chaperones began during his time at the Ludwig Maximilian University of Munich. Soon after he arrived at Munich in 1985, the scientific field confirmed that proteins inside cells had to unfold before and crossing the mitochondrial membrane to enter mitochondria and then refold afterwards, and that heat shock proteins interacted with proteins before they crossed the mitochondrial or the cell membrane.[10] This made the mitochondria a nice model to study protein folding. However, the long-held belief was that proteins fold spontaneously.[11]

Walter Neupert, the Ludwig Maximilian University of Munich professor under Hartl was working, introduced Hartl to Arthur L. Horwich. Using a mutant strain of yeast that could import a certain protein (ornithine transcarbamylase) into the mitochondria but the protein could not fold or become functional once inside the mitochondria. They found the gene mutated in this mutant strain was identical to a previously discovered gene, HSP60.[12] The HSP60 protein, encoded by the HSP60 gene, belongs to a family of chaperones called chaperonin.

Next, Hartl and Horwich investigated how the HSP60 protein helped proteins fold. They looked at another protein, dihydrofolate reductase, in Neurospora crassa, a fungus species, and found ATP, the energy currency in cells, is required for the HSP60 protein helping other proteins fold. Their finding showed HSP60-mediated protein folding is dependent on energy.[13]

Hartl continued studying chaperones and protein folding after moving to the Memorial Sloan Kettering Cancer Center, focusing on the mechanism by which chaperones helping other proteins fold. He turned to the E. coli counterpart of the eukaryotic HSP60 protein, known as GroEL, and its helper protein GroES. His group showed chaperone-mediated folding actually consisted of a series of steps, and that multiple chaperones passed off partially folded proteins from one to the next.[14] His group also found GroEL and GroES together formed a cage inside which the target protein was trapped and folded.[15][16]

More recently, Hartl's work expanded to proteostasis, which a cell's regulation of protein biosynthesis, protein folding, protein trafficking, and protein degradation, and how abnormalities in proteostasis can cause protein aggregation and diseases.[17][18]

 
Scholia has an author profile for Franz-Ulrich Hartl.

Personal life

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Hartl is married to Manajit Hayer-Hartl, whom he met in 1986 at a molecular biology summer school on a Greek island. Hayer-Hartl is currently a research group leader at the Max Planck Institute of Biochemistry[19] and a close collaborator of Hartl since 1991.[10] She was awarded the ASBMB-Merck Award in 2021.[20]

Honours and awards

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References

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  1. ^ a b c d e f "Curriculum Vitae". Max Planck Institute of Biochemistry. Archived from the original on 11 September 2023. Retrieved 11 September 2023.
  2. ^ a b c d e "Autobiography of Franz-Ulrich Hartl". Shaw Prize. Archived from the original on 22 July 2023. Retrieved 22 July 2023.
  3. ^ "Eiwitklonten en spaghettislierten" (PDF) (in German). Heineken Prizes. Archived from the original (PDF) on 11 September 2023. Retrieved 11 September 2023.
  4. ^ "FREQUENTLY ASKED QUESTIONS: HABILITATION" (PDF). Zeppelin University. Archived from the original (PDF) on 11 September 2023. Retrieved 11 September 2023.
  5. ^ "Habilitation". Leipzig University. Archived from the original on 11 September 2023. Retrieved 11 September 2023.
  6. ^ "Organization of the Institute". Max Planck Institute of Biochemistry. Archived from the original on 12 September 2023. Retrieved 12 September 2023.
  7. ^ "Organization of the Institute". Max Planck Institute of Biochemistry. Archived from the original on 7 December 2022. Retrieved 7 December 2022.
  8. ^ "Franz-Ulrich Hartl, MD". Howard Hughes Medical Institute. Archived from the original on 12 September 2023. Retrieved 12 September 2023.
  9. ^ Kim, Yujin E.; Hipp, Mark S.; Bracher, Andreas; Hayer-Hartl, Manajit; Hartl, F. Ulrich (2013). "Molecular Chaperone Functions in Protein Folding and Proteostasis". Annual Review of Biochemistry. 82: 323–355. doi:10.1146/annurev-biochem-060208-092442. PMID 23746257. Retrieved 18 September 2023.
  10. ^ a b Hartl, F. Ulrich (2011). "Chaperone-assisted protein folding: the path to discovery from a personal perspective" (PDF). Nature Medicine. 17 (10): 1206–1210. doi:10.1038/nm.2467. PMID 21989011. S2CID 4827124. Archived from the original (PDF) on 19 September 2023. Retrieved 18 September 2023.
  11. ^ Claiborn, Kathryn (2011). "A mystery unfolds: Franz-Ulrich Hartl and Arthur L. Horwich win the 2011 Albert Lasker Basic Medical Research Award". Journal of Clinical Investigation. 121 (10): 3774–3777. doi:10.1172/JCI60889. PMC 3195494. PMID 22059237. Archived from the original on 18 September 2023. Retrieved 18 September 2023.
  12. ^ Cheng, Ming Y.; Hartl, F.-Ulrich; Martin, Jörg; Pollock, Robert A.; Kalousek, Frantisek; Neupert, Walter; Hallberg, Elizabeth M.; Hallberg, Richard L.; Horwich, Arthur L. (1989). "Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria". Nature. 337 (6208): 620–625. Bibcode:1989Natur.337..620C. doi:10.1038/337620a0. PMID 2645524. S2CID 4333381. Retrieved 18 September 2023.
  13. ^ Ostermann, Joachim; Horwich, Arthur L.; Neupert, Walter; Hartl, F.-Ulrich (1989). "Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis". Nature. 341 (6238): 125–130. Bibcode:1989Natur.341..125O. doi:10.1038/341125a0. PMID 2528694. S2CID 1552845. Retrieved 18 September 2023.
  14. ^ Langer, Thomas; Lu, Chi; Echols, Harrison; Flanagan, John; Hayer, Manajit K.; Hartl, F. Ulrich (1992). "Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding". Nature. 356 (6371): 683–689. Bibcode:1992Natur.356..683L. doi:10.1038/356683a0. PMID 1349157. S2CID 4324738. Retrieved 20 September 2023.
  15. ^ Langer, Thomas; Pfeifer, Gunter; Martin, Jörg; Baumeister, Wolfgang; Hartl, Franz-Ulrich (1992). "Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity". The EMBO Journal. 11 (13): 4757–4765. doi:10.1002/j.1460-2075.1992.tb05581.x. PMC 556951. PMID 1361169.
  16. ^ Martin, Jörg; Mayhew, Mark; Langer, Thomas; Hartl, Ulrich (1993). "The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding". Nature. 366 (6452): 228–233. Bibcode:1993Natur.366..228M. doi:10.1038/366228a0. PMID 7901770. S2CID 4361040. Retrieved 20 September 2023.
  17. ^ Woerner, Andreas C.; Frottin, Frédéric; Hornburg, Daniel; Feng, Li R.; Meissner, Felix; Patra, Maria; Tatzelt, Jörg; Mann, Matthias; Winklhofer, Konstanze F.; Hartl, F. Ulrich; Hipp, Mark S. (2016). "Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA". Science. 351 (6269): 173–176. Bibcode:2016Sci...351..173W. doi:10.1126/science.aad2033. hdl:11858/00-001M-0000-002B-0491-8. PMID 26634439. S2CID 206642264. Retrieved 21 September 2023.
  18. ^ Kim, Yujin E.; Hosp, Fabian; Frottin, Frédéric; Ge, Hui; Mann, Matthias; Hayer-Hartl, Manajit; Hartl, F. Ulrich (2016). "Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors". Molecular Cell. 63 (6): 951–964. doi:10.1016/j.molcel.2016.07.022. PMID 27570076.
  19. ^ "Manajit Hayer-Hartl". Max Planck Institute of Biochemistry. Archived from the original on 19 September 2023. Retrieved 19 September 2023.
  20. ^ Stivison, Elizabeth (1 November 2019). "Winding path leads to plant enzyme breakthrough". ASBMB Today. American Society for Biochemistry and Molecular Biology. Archived from the original on 19 September 2023. Retrieved 19 September 2023.
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  27. ^ "F. Ulrich Hartl". Gairdner Foundation. Archived from the original on 13 September 2023. Retrieved 13 September 2023.
  28. ^ "Laureates 1976 to 2022". Ernst Jung Foundation. Archived from the original on 14 August 2023. Retrieved 14 August 2023.
  29. ^ "Protein Society Awards". Protein Society. Archived from the original on 13 September 2023. Retrieved 13 September 2023.
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  33. ^ "2010 - 2001 Awardees". Columbia University. 11 November 2022. Archived from the original on 14 September 2023. Retrieved 14 September 2023.
  34. ^ "Prize Winners of the Paul Ehrlich and Ludwig Darmstaedter Prize 2019". Goethe University Frankfurt. Archived from the original on 14 September 2023. Retrieved 14 September 2023.
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  37. ^ "Ministerpräsident Seehofer händigt Bayerischen Verdienstorden und Bundesverdienstkreuz an verdiente Persönlichkeiten aus" (Press release) (in German). Government of Bavaria. 22 March 2011. Archived from the original on 17 February 2017. Retrieved 17 February 2017.
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  43. ^ "The 2012 Prize in Life Science & Medicine". Shaw Prize. Archived from the original on 15 September 2023. Retrieved 15 September 2023.
  44. ^ Eisen, Jonathan A. (1 March 2012). "Full list of 2012 American Academy of Microbiology Fellows Announced". University of California, Davis. Archived from the original on 15 September 2023. Retrieved 15 September 2023.
  45. ^ "F.-Ulrich Hartl receives Herbert Tabor Research Award" (Press release). Max Planck Institute of Biochemistry. 19 April 2013. Archived from the original on 15 September 2023. Retrieved 15 September 2023.
  46. ^ "Previous Recipients". Albany Medical Center. Archived from the original on 26 November 2021. Retrieved 26 November 2021.
  47. ^ "Franz-Ulrich Hartl Ernst: Schering Prize 2016". Ernst Schering Foundation. Archived from the original on 15 September 2023. Retrieved 15 September 2023.
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  49. ^ Spiro, Mary (22 September 2017). "Hartl and Horwich named 2017 E.B. Wilson Medalists". American Society for Cell Biology. Archived from the original on 15 September 2023. Retrieved 15 September 2023.
  50. ^ "A German biochemist wins this year's Debrecen Award". University of Debrecen. 13 December 2017. Archived from the original on 16 September 2023. Retrieved 16 September 2023.
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  55. ^ "2022 - Franz-Ulrich Hartl and Arthur L. Horwich". Human Frontier Science Program. Archived from the original on 16 September 2023. Retrieved 16 September 2023.
  56. ^ "Schleiden Medal". German National Academy of Sciences Leopoldina. Archived from the original on 16 September 2023. Retrieved 16 September 2023.
  57. ^ BBVA Foundation Frontiers of Knowledge Award 2023
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