| pubmed-article:9973396 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C0036971 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C1416447 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:9973396 | lifeskim:mentions | umls-concept:C0163342 | lld:lifeskim |
| pubmed-article:9973396 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9973396 | pubmed:dateCreated | 1999-4-13 | lld:pubmed |
| pubmed-article:9973396 | pubmed:abstractText | Our recent studies revealed that the inositol phosphatase Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP) is phosphorylated and associated with Shc exclusively under negative signaling conditions in B cells, which is due to recruitment of the SHIP SH2 domain to the FcgammaRIIb. In addition, we reported that SHIP-Shc interaction involves both SHIP SH2 and Shc phosphotyrosine binding domains. These findings reveal a paradox in which the single SH2 domain of SHIP is simultaneously engaged to two different proteins: Shc and FcgammaRIIb. To resolve this paradox, we examined the protein interactions of SHIP. Our results demonstrated that isolated FcgammaRIIb contains SHIP but not Shc; likewise, Shc isolates contain SHIP but not FcgammaRIIb. In contrast, SHIP isolates contain both proteins, revealing two separate pools of SHIP: one bound to FcgammaRIIb and one bound to Shc. Kinetic studies reveal rapid SHIP association with FcgammaRIIb but slower and more transient association with Shc. Affinity measurements using a recombinant SHIP SH2 domain and phosphopeptides derived from FcgammaRIIb (corresponding to Y273) and Shc (corresponding to Y317) revealed an approximately equal rate of binding but a 10-fold faster dissociation rate for FcgammaRIIb compared with Shc phosphopeptide and yielding in an affinity of 2.1 microM for FcgammaRIIb and 0.26 microM for Shc. These findings are consistent with a model in which SHIP transiently associates with FcgammaRIIb to promote SHIP phosphorylation, whereupon SHIP binds to Shc and dissociates from FcgammaRIIb. | lld:pubmed |
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| pubmed-article:9973396 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9973396 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9973396 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9973396 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:9973396 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9973396 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9973396 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:9973396 | pubmed:author | pubmed-author:AndersonC LCL | lld:pubmed |
| pubmed-article:9973396 | pubmed:author | pubmed-author:GarberSS | lld:pubmed |
| pubmed-article:9973396 | pubmed:author | pubmed-author:PradhanMM | lld:pubmed |
| pubmed-article:9973396 | pubmed:author | pubmed-author:CoggeshallK... | lld:pubmed |
| pubmed-article:9973396 | pubmed:author | pubmed-author:LaDineJ RJR | lld:pubmed |
| pubmed-article:9973396 | pubmed:author | pubmed-author:TridandapaniS... | lld:pubmed |
| pubmed-article:9973396 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9973396 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9973396 | pubmed:volume | 162 | lld:pubmed |
| pubmed-article:9973396 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9973396 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9973396 | pubmed:pagination | 1408-14 | lld:pubmed |
| pubmed-article:9973396 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9973396 | pubmed:meshHeading | pubmed-meshheading:9973396-... | lld:pubmed |
| pubmed-article:9973396 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9973396 | pubmed:articleTitle | Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): association with Shc displaces SHIP from FcgammaRIIb in B cells. | lld:pubmed |
| pubmed-article:9973396 | pubmed:affiliation | Department of Microbiology, Ohio State University, OH 43210, USA. | lld:pubmed |
| pubmed-article:9973396 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9973396 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9973396 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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