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| pubmed-article:8611507 | lifeskim:mentions | umls-concept:C1956003 | lld:lifeskim |
| pubmed-article:8611507 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:8611507 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:8611507 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8611507 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
| pubmed-article:8611507 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:8611507 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:8611507 | pubmed:dateCreated | 1996-6-6 | lld:pubmed |
| pubmed-article:8611507 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8611507 | pubmed:abstractText | The cDNA encoding human brain protein phosphatase inhibitor-1 (I-1) was expressed in Escherichia coli. Following PKA phosphorylation at a threonine, recombinant human I-1 was indistinguishable from rabbit skeletal muscle I-1 as a potent and specific inhibitor of the type-1 protein serine/threonine phosphatase (PP1). N-Terminal phosphopeptides of I-1 that retained the selectivity of intact human I-1 highlighted a functional domain that mediates PP1 inhibition. Substituting alanine in place of threonine-36 eliminated I-1 phosphorylation by PKA and its phosphatase inhibitor activity. An acidic residue was substituted in place of the phosphoacceptor to produce I-1(T35D), a constitutive phosphate inhibitor. I-1(T35D) was an equally effective inhibitor of PP1 and the type-2 phosphatase, PP2A. However, CNbr digestion of I-1(T35D) yielded an N-terminal peptide that showed 100-fold increased specificity as a PP1 inhibitor. This provided new insight into a unique conformation of the phosphorylated I-1 that accounts for selective inhibition of PP1 activity. Truncation of an active I-1 phosphopeptide identified an N-terminal sequence that was reduced in addition to threonine-35 phosphorylation to inhibit PP1 activity. Biosensor studies demonstrated that PP1 bound to both Phosphorylated and dephosphorylated I-1 and suggested that distinct elements of I-1 structure accounted for PP1 binding and inhibition. Our data point to multiple interactions between the I-1 functional domain. and the PP1 catalytic subunit that define this phosphoprotein as a physiological regulator of the type-1 protein phosphatase. | lld:pubmed |
| pubmed-article:8611507 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8611507 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8611507 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8611507 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8611507 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8611507 | pubmed:author | pubmed-author:EndoSS | lld:pubmed |
| pubmed-article:8611507 | pubmed:author | pubmed-author:ZhouXX | lld:pubmed |
| pubmed-article:8611507 | pubmed:author | pubmed-author:ShenolikarSS | lld:pubmed |
| pubmed-article:8611507 | pubmed:author | pubmed-author:ConnorJJ | lld:pubmed |
| pubmed-article:8611507 | pubmed:author | pubmed-author:WandAA | lld:pubmed |
| pubmed-article:8611507 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8611507 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:8611507 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:8611507 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8611507 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8611507 | pubmed:pagination | 5220-8 | lld:pubmed |
| pubmed-article:8611507 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:8611507 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8611507 | pubmed:articleTitle | Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor. | lld:pubmed |
| pubmed-article:8611507 | pubmed:affiliation | Department of Pharmacology, Duke University Medical Center, Durham, North Carolina 27708, USA. | lld:pubmed |
| pubmed-article:8611507 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8611507 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8611507 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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