Identification of a 14 - 3 - 3 Protein from with CAP ( Adenylyl Cyclase - associated of This Interaction in Fission Yeast Lentinus edodes That Interacts Protein ) , and Conservation
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چکیده
morphology and UY sensitiyity, suggesting functional conseryation of 14-3-3 proteins between L. edodes and S. pombe. The interactien between L. edodes CAP and 14-3-3 protein was restricted to the IV-terminal domain of CAP and was confirmed by in vitro co-precipitation. Results from both the two-hybrid system and in vivo co-precipitation experiments showed the conservation of this interactien in S. pombe. The obseryation that a 14-3-3 protein interacts with the IVLterrninal portion of
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اندازهگیری فعالیت آدنیلیل سیکلاز غشاء سلولی در حضور پروتئین کموتاکسیک ماکروفاژ
Adenylyl cyclase is a membrane-bound enzyme that catalyzes the conversion of ATP to cAMP. The inhibition of adenylyl cyclase was carried out by measuring the ability of the macrophage chemotactic protein-1 to inhibit the forskolin-induced enzyme activity. Measurement of adenylyl cyclase activity was performed according to the procedure described by Wiegn. Adenylyl cyclase activity in the pres...
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We previously reported the identification of human CAP, a protein that is related to the Saccharomyces cerevisiae and Schizosaccharomyces pombe adenylyl cyclase-associated CAP proteins. The two yeast CAP proteins have similar functions: the N-terminal domains are required for the normal function of adenylyl cyclase, while loss of the C-terminal domains result in morphological and nutritional de...
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CAP, an adenylyl cyclase associated protein, is present in Saccharomyces cerevisiae and Schizosaccharomyces pombe. In both organisms, CAP is bifunctional: the N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to respond appropriately to upstream regulatory signals, such as RAS in S. cerevisiae; the C-terminal domain is required for cellular morphogenesis. Here, we d...
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We have isolated a rat cDNA whose expression suppresses the physiological consequences of the chromosomal disruption of CAP, the gene encoding the adenylyl cyclase-associated protein of Saccharomyces cerevisiae. Yeast CAP is a bifunctional protein: the NH2 terminus is necessary and sufficient for cellular responsiveness to activated RAS proteins, while the COOH terminus is required for normal c...
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Cyclase-associated protein (CAP) is an evolutionarily conserved regulator of the G-actin/F-actin ratio and, in yeast, is involved in regulating the adenylyl cyclase activity. We show that cell polarization, F-actin organization, and phototaxis are altered in a Dictyostelium CAP knockout mutant. Furthermore, in complementation assays we determined the roles of the individual domains in signaling...
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