| pubmed-article:20624911 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20624911 | lifeskim:mentions | umls-concept:C0178453 | lld:lifeskim |
| pubmed-article:20624911 | lifeskim:mentions | umls-concept:C0021547 | lld:lifeskim |
| pubmed-article:20624911 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:20624911 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
| pubmed-article:20624911 | lifeskim:mentions | umls-concept:C0071653 | lld:lifeskim |
| pubmed-article:20624911 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:20624911 | pubmed:dateCreated | 2010-8-25 | lld:pubmed |
| pubmed-article:20624911 | pubmed:abstractText | The ability to undergo dramatic morphological changes in response to extrinsic cues is conserved in fungi. We have used the model yeast Schizosaccharomyces pombe to determine which intracellular signal regulates the dimorphic switch from the single-cell yeast form to the filamentous invasive growth form. The S. pombe Asp1 protein, a member of the conserved Vip1 1/3 inositol polyphosphate kinase family, is a key regulator of the morphological switch via the cAMP protein kinase A (PKA) pathway. Lack of a functional Asp1 kinase domain abolishes invasive growth which is monopolar, while an increase in Asp1-generated inositol pyrophosphates (PP) increases the cellular response. Remarkably, the Asp1 kinase activity encoded by the N-terminal part of the protein is regulated negatively by the C-terminal domain of Asp1, which has homology to acid histidine phosphatases. Thus, the fine tuning of the cellular response to environmental cues is modulated by the same protein. As the Saccharomyces cerevisiae Asp1 ortholog is also required for the dimorphic switch in this yeast, we propose that Vip1 family members have a general role in regulating fungal dimorphism. | lld:pubmed |
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| pubmed-article:20624911 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20624911 | pubmed:citationSubset | IM | lld:pubmed |
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