| pubmed-article:18541533 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C0237401 | lld:lifeskim |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C0018358 | lld:lifeskim |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C0035331 | lld:lifeskim |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C1415364 | lld:lifeskim |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:18541533 | lifeskim:mentions | umls-concept:C1578593 | lld:lifeskim |
| pubmed-article:18541533 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:18541533 | pubmed:dateCreated | 2008-7-28 | lld:pubmed |
| pubmed-article:18541533 | pubmed:abstractText | Guanylyl cyclase activating protein 1 (GCAP1), after substitution of Ca(2+) by Mg(2+) in its EF-hands, stimulates photoreceptor guanylyl cyclase, RetGC1, in response to light. We inactivated metal binding in individual EF-hands of GCAP1 tagged with green fluorescent protein to assess their role in GCAP1 binding to RetGC1 in co-transfected HEK293 cells. When expressed alone, GCAP1 was uniformly distributed throughout the cytoplasm and the nuclei of the cells, but when co-expressed with either fluorescently tagged or non-tagged RetGC1, it co-localized with the cyclase in the membranes. The co-localization did not occur when the C-terminal portion of RetGC1, containing its regulatory and catalytic domains, was removed. Mutations that preserved Mg(2+) binding in all three metal-binding EF-hands did not affect GCAP1 association with the cyclase in live cells. Locking EF-hand 4 in its apo-conformation, incapable of binding either Ca(2+) or Mg(2+), had no effect on GCAP1 association with the cyclase. In contrast to EF-hand 4, inactivation of EF-hand 3 reduced the efficiency of the co-localization, and inactivation of EF-hand 2 drastically suppressed GCAP1 binding to the cyclase. These results directly demonstrate that metal binding in EF-hand 2 is crucial for GCAP1 attachment to RetGC1, and that in EF-hand 3 it is less critical, although it enhances the efficiency of the GCAP1 docking on the target enzyme. Metal binding in EF-hand 4 has no role in the primary attachment of GCAP1 to the cyclase, and it only triggers the activator-to-inhibitor functional switch in GCAP1. | lld:pubmed |
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| pubmed-article:18541533 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18541533 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18541533 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18541533 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18541533 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18541533 | pubmed:author | pubmed-author:OlshevskayaEl... | lld:pubmed |
| pubmed-article:18541533 | pubmed:author | pubmed-author:DizhoorAlexan... | lld:pubmed |
| pubmed-article:18541533 | pubmed:author | pubmed-author:PeshenkoIgor... | lld:pubmed |
| pubmed-article:18541533 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18541533 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18541533 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18541533 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18541533 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18541533 | pubmed:pagination | 21747-57 | lld:pubmed |
| pubmed-article:18541533 | pubmed:dateRevised | 2011-5-30 | lld:pubmed |
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| pubmed-article:18541533 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18541533 | pubmed:articleTitle | Binding of guanylyl cyclase activating protein 1 (GCAP1) to retinal guanylyl cyclase (RetGC1). The role of individual EF-hands. | lld:pubmed |
| pubmed-article:18541533 | pubmed:affiliation | Hafter Research Laboratories, Pennsylvania College of Optometry, 8360 Old York Road, Elkins Park, PA 19027, USA. | lld:pubmed |
| pubmed-article:18541533 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18541533 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18541533 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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