TY - JOUR
T1 - Remarkable similarities between yeast and mammalian protein phosphatases
AU - Cohen, Philip
AU - Schelling, Donald L.
AU - Stark, Michael J. R.
PY - 1989/7/3
Y1 - 1989/7/3
N2 - Protein phosphatase activities in extracts of the yeast Saccharomyces cerevisiae showed remarkable similarities to the mammalian type 1, type 2A and type 2C enzymes. Similarities included their substrate specificities, including selectivity for the a- and ß-subunits of muscle phosphorylase kinase, sensitivity to okadaic acid and to mammalian inhibitor 1 and inhibitor 2, and requirement for divalent cations. The results suggest that the function and regulation of these enzymes has been highly conserved during evolution and indicate that the improved procedure for identifying and quantitating protein phosphatases [(1989) FEBS Lett. 250, 000-000] may be applicable to all eukaryotic cells.
AB - Protein phosphatase activities in extracts of the yeast Saccharomyces cerevisiae showed remarkable similarities to the mammalian type 1, type 2A and type 2C enzymes. Similarities included their substrate specificities, including selectivity for the a- and ß-subunits of muscle phosphorylase kinase, sensitivity to okadaic acid and to mammalian inhibitor 1 and inhibitor 2, and requirement for divalent cations. The results suggest that the function and regulation of these enzymes has been highly conserved during evolution and indicate that the improved procedure for identifying and quantitating protein phosphatases [(1989) FEBS Lett. 250, 000-000] may be applicable to all eukaryotic cells.
U2 - 10.1016/0014-5793(89)80804-X
DO - 10.1016/0014-5793(89)80804-X
M3 - Article
SN - 0014-5793
VL - 250
SP - 601
EP - 606
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -