Figure 1.

Four Nobel Prizes in Physiology or Medicine awarded in the field of protein phosphorylation and protein kinases. Protein kinases catalyze the transfer of the γ-phosphate of ATP to the hydroxyl substituents of serine, threonine, or tyrosine residues in proteins, thereby altering the physiological properties of their protein substrates. The human kinome comprises 538 protein kinases. Michael Bishop and Harold E. Varmus received the Nobel Prize 1989 “for their discovery of the cellular origin of retroviral oncogenes” (src, the first described oncogene, which encodes a tyrosine kinase). Edmond H. Fischer and Edwin G. Krebs received the Nobel Prize 1992 “for their discoveries concerning reversible protein phosphorylation as a biological regulatory mechanism” (they are the true discoverers of protein kinases). The Nobel Prize 2000 was awarded jointly to Arvid Carlsson, Paul Greengard, and Eric R. Kandel “for their discoveries concerning signal transduction in the nervous system” (Paul Greengard investigated the mechanism of signal transduction of neurotransmitters in the central nervous system and demonstrated the key importance of phosphorylation by kinases such as CDK5, PKA, CK1, and CK2 and Eric Kandel the importance of PKA in memory in Aplysia). The Nobel Prize 2001 was awarded jointly to Leland H. Hartwell, Tim Hunt, and Paul M. Nurse “for their discoveries of key regulators of the cell cycle” (using yeast or sea urchin embryos, they discovered how the cell division cycle is regulated by CDKs). For more information on each of these awardees, see: https://www.nobelprize.org/prizes/medicine/ (accessed on 1 June 2021).