P4-129 Genetic study of APH-1 and PEN-2, components of presenilin high molecular weight complex

2004 ◽  
Vol 25 ◽  
pp. S512
Author(s):  
Toshitaka Kawarai ◽  
Antonio Orlacchio ◽  
Ekaterina Rogaeva ◽  
Susan Ling ◽  
Hiroshi Hasegawa ◽  
...  
1991 ◽  
Vol 7 (1) ◽  
pp. 63-69 ◽  
Author(s):  
D. V. Gnatenko ◽  
A. I. Kornelyuk ◽  
I. V. Kurochkin ◽  
G. H. Matsuka

1992 ◽  
Vol 12 (11) ◽  
pp. 4937-4945
Author(s):  
J Wang ◽  
N Suzuki ◽  
T Kataoka

In the yeast Saccharomyces cerevisiae, adenylyl cyclase is regulated by RAS proteins. We show here that the yeast adenylyl cyclase forms at least two high-molecular-weight complexes, one with the RAS protein-dependent adenylyl cyclase activity and the other with the Mn(2+)-dependent activity, which are separable by their size difference. The 70-kDa adenylyl cyclase-associated protein (CAP) existed in the former complex but not in the latter. Missense mutations in conserved motifs of the leucine-rich repeats of the catalytic subunit of adenylyl cyclase abolished the RAS-dependent activity, which was accompanied by formation of a very high molecular weight complex having the Mn(2+)-dependent activity. Contrary to previous results, disruption of the gene encoding CAP did not alter the extent of RAS protein-dependent activation of adenylyl cyclase, while a concomitant decrease in the size of the RAS-responsive complex was observed. These results indicate that CAP is not essential for interaction of the yeast adenylyl cyclase with RAS proteins even though it is an inherent component of the RAS-responsive adenylyl cyclase complex.


2001 ◽  
Vol 277 (6) ◽  
pp. 3926-3934 ◽  
Author(s):  
Paul A. Price ◽  
Gethin R. Thomas ◽  
Aaron W. Pardini ◽  
William F. Figueira ◽  
Jeffrey M. Caputo ◽  
...  

2001 ◽  
Vol 127 (3) ◽  
pp. 1243-1255 ◽  
Author(s):  
Yong-Woo Kim ◽  
Dae-Sup Park ◽  
Seung-Cheol Park ◽  
Sung Hee Kim ◽  
Gang-Won Cheong ◽  
...  

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