| pubmed-article:14567754 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14567754 | lifeskim:mentions | umls-concept:C0021554 | lld:lifeskim |
| pubmed-article:14567754 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:14567754 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:14567754 | pubmed:dateCreated | 2004-1-5 | lld:pubmed |
| pubmed-article:14567754 | pubmed:abstractText | This review assesses the extent and the significance of catalytic versatility shown by several inositol phosphate kinases: the inositol phosphate multikinase, the reversible Ins(1,3,4) P (3)/Ins(3,4,5,6) P (4) kinase, and the kinases that synthesize diphosphoinositol polyphosphates. Particular emphasis is placed upon data that are relevant to the situation in vivo. It will be shown that catalytic promiscuity towards different inositol phosphates is not typically an evolutionary compromise, but instead is sometimes exploited to facilitate tight regulation of physiological processes. This multifunctionality can add to the complexity with which inositol signalling pathways interact. This review also assesses some proposed additional functions for the catalytic domains, including transcriptional regulation, protein kinase activity and control by molecular 'switching', all in the context of growing interest in 'moonlighting' (gene-sharing) proteins. | lld:pubmed |
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