Linked Life Data

9973396

Source:http://linkedlifedata.com/resource/pubmed/id/9973396

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-4-13
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1408-14
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9973396-Adaptor Proteins, Signal Transducing, pubmed-meshheading:9973396-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:9973396-Animals, pubmed-meshheading:9973396-B-Lymphocytes, pubmed-meshheading:9973396-Binding Sites, pubmed-meshheading:9973396-Cell Line, pubmed-meshheading:9973396-Kinetics, pubmed-meshheading:9973396-Macromolecular Substances, pubmed-meshheading:9973396-Mice, pubmed-meshheading:9973396-Models, Biological, pubmed-meshheading:9973396-Phosphoric Monoester Hydrolases, pubmed-meshheading:9973396-Phosphorylation, pubmed-meshheading:9973396-Protein Binding, pubmed-meshheading:9973396-Proteins, pubmed-meshheading:9973396-Receptors, IgG, pubmed-meshheading:9973396-Recombinant Proteins, pubmed-meshheading:9973396-Shc Signaling Adaptor Proteins, pubmed-meshheading:9973396-src Homology Domains
pubmed:year
1999
pubmed:articleTitle
Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): association with Shc displaces SHIP from FcgammaRIIb in B cells.
pubmed:affiliation
Department of Microbiology, Ohio State University, OH 43210, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't