The serine-/threonine-specific protein phosphatase calcineurin is conserved from yeast to man and was first detected in bovine brain extracts by Wang and Desai and independently by Watterson and Vanaman in 1976 (Wang and Desai 1976; Watterson and Vanaman 1976). Klee and Krinks were the first to purify calcineurin in 1978 (Klee and Krinks 1978), and Klee also coined the name “calcineurin,” since the protein was extracted from brain tissue and it could bind Ca2+ (Klee et al. 1979). However, the function of calcineurin was not known at this time. It was assumed that calcineurin might be a regulatory subunit of the phosphodiesterase, as it could inhibit phosphodiesterase activity. In the early 1980s, the real function as a phosphatase was demonstrated. Stewart et al. found that the protein phosphatase 2B isolated from rabbit skeletal muscle was identical to the previously identified calcineurin...
KeywordsDown Syndrome Lower Eukaryote Calcineurin Activity Autoinhibitory Domain Amoeba Dictyostelium Discoideum
- Adler A, Park YD, Larsen P, Nagarajan V, Wollenberg K, Qiu J, et al. A novel specificity protein 1 (SP1)-like gene regulating protein kinase C-1 (Pkc1)-dependent cell wall integrity and virulence factors in Cryptococcus neoformans. J Biol Chem. 2011;286(23):20977–90.CrossRefPubMedPubMedCentralGoogle Scholar
- Thewes S. The role of calcineurin during development: parallels and differences between higher and lower eukaryotes. Cell News. 2014b;40(4):10–6.Google Scholar