Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 17(102), p. 6108-6113, 2005

DOI: 10.1073/pnas.0502270102

Links

Tools

Export citation

Search in Google Scholar

Direct activation of fission yeast adenylate cyclase by the Gpa2 Gα of the glucose signaling pathway

Journal article published in 2005 by F. Douglas Ivey, F. Douglas Ivey, Charles S. Hoffman ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Red circle
Preprint: archiving forbidden
Green circle
Postprint: archiving allowed
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

G protein-mediated signaling is implicated in yeast and fungal cAMP pathways. By two-hybrid screens and pull-down experiments, we show that the fission yeast Gpa2 Galpha binds an N-terminal domain of adenylate cyclase, comprising a moderately conserved sequence within a region otherwise poorly related to other fungal adenylate cyclases. Overexpressing this domain in yeast perturbs cAMP signaling, which is restored by Gpa2 coexpression. Mutations affecting this domain, over 1,100 residues from the catalytic domain, alter glucose-triggered cAMP signaling. This is evidence for direct activation of adenylate cyclase by a fungal G protein and suggests a distinct activation mechanism from that of mammals.