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CDC25 ‐dependent induction of inositol 1,4,5‐trisphosphate and diacylglycerol in Saccharomyces cerevisiae by nitrogen
Author(s) -
Schomerus Christof,
Küntzel Hans
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80688-d
Subject(s) - diacylglycerol kinase , inositol , second messenger system , adenylyl cyclase , biochemistry , phospholipase c , diglyceride , biology , pi , sugar phosphates , camp dependent pathway , inositol trisphosphate , cdc25 , saccharomyces cerevisiae , inositol phosphate , chemistry , signal transduction , yeast , protein kinase c , gene , receptor , enzyme , cell cycle , cyclin dependent kinase 1
The addition of ammonium sulfate to starved yeast cells leads to a 3‐ to 4‐fold rapid increase of the second messengers inositol 1,4,5‐trisphosphate (IP 3 ) and diacylglycerol (DAG), the products of phosphoinositide‐specific phospholipase C (PI‐PLC). This response is reduced by dissecting the RAS‐activating Cdc25 protein, and is completely abolished by the cdc25‐1 mutation even at permissive temperature. Starved cdc25‐1 mutant cells have a strongly reduced IP 3 content, but an at least 10‐fold increased DAG level compared to the isogenic wild‐type strain. NH 4 does not stimulate cAMP synthesis, and glucose does not induce IP 3 and DAG. Our data suggest that the Cdc25 protein controls a nitrogen‐specific signalling pathway involving the effector PI‐PLC, in addition to the glucose‐induced activation of adenylyl cyclase (AC).