Glucose-induced degradation of yeast fructose-1,6-bisphosphatase requires additional triggering events besides protein phosphorylation.
FEBS Lett
; 216(2): 265-9, 1987 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-3034678
ABSTRACT
Glucose addition to yeast cells stimulates a cAMP overshoot with concomitant activation of cAMP-dependent protein kinase, which in turn rapidly phosphorylates fructose-1,6-bisphosphatase. The phosphorylated enzyme subsequently undergoes a slow proteolytic breakdown. Also, it has been proposed that phosphorylation represents the mechanism that initiates proteolysis. Here we present experiments carried out on a yeast mutant defective in adenylate cyclase [(1982) Proc. Natl. Acad. Sci. USA 79, 2355-2359] in which extracellular cAMP triggers full enzyme phosphorylation but a scanty proteolysis, whereas glucose plus cAMP provoke both phosphorylation and complete proteolytic breakdown. Thus, besides a glucose-induced cAMP peak, which results in enzyme phosphorylation, other effects evoked by the sugar are indispensable for its proteolytic degradation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfoproteínas
/
Frutose-Bifosfatase
/
Glucose
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1987
Tipo de documento:
Article