Regulation of the adenylate cyclase system in the lungs of rats treated with plague toxin

1994 ◽  
Vol 117 (3) ◽  
pp. 280-282 ◽  
Author(s):  
T. D. Cherkasova ◽  
V. A. Yurkiv ◽  
V. I. Pokrovskii
1975 ◽  
Vol 250 (4) ◽  
pp. 1186-1192
Author(s):  
F M Finn ◽  
J A Montibeller ◽  
Y Ushijima ◽  
K Hofmann

1972 ◽  
Vol 247 (7) ◽  
pp. 2038-2043 ◽  
Author(s):  
Lutz Birnbaumer ◽  
Stephen L. Pohl ◽  
Martin Rodbell ◽  
Finn Sundby

1980 ◽  
Vol 255 (22) ◽  
pp. 10841-10846 ◽  
Author(s):  
P.M. Lad ◽  
T.B. Nielsen ◽  
C. Londos ◽  
M.S. Preston ◽  
M. Rodbell

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.


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