Document Detail


Regulation of the association between PSTPIP and CD2 in murine T cells.
MedLine Citation:
PMID:  11599917     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Prominent in T cells and natural killer cells, CD2 binding protein 1 (CD2BP1) plays an important role in CD2-mediated adhesion and signal transduction. In the current study, we investigated CD2 and PSTPIP (proline, serine, threonine phosphatase interacting protein, murine homologue of CD2BP1) interactions in purified mouse splenic T cells. PSTPIP associated with CD2 in both resting and activated T cells. Following various stimuli, such as concanavalin A, anti-TCRbeta, anti-CD3epsilon, anti-CD3epsilon/phorbol myristate acetate (PMA), IL-2, or PMA/ionomycin, PSTPIP and CD2 expression, as well as their association, increased in a time-dependent fashion. While PSTPIP expression and CD2 expression were comparable across most groups, the PSTPIP-CD2 association stimulated by anti-CD3epsilon alone was significantly greater than with other stimuli. Stimulation by anti-CD3epsilon plus anti-CD28 induced even greater PSTPIP-CD2 association than anti-CD3epsilon treatment alone, indicating that CD28 initiated signals are involved in regulating this interaction. There was no direct association between CD3epsilon or CD28 and PSTPIP. Tyrosine phosphorylated PSTPIP bound poorly to CD2 compared to dephosphorylated PSTPIP, and protein tyrosine phosphatase was shown to affect both phosphorylation of PSTPIP and the CD2-PSTPIP association. In addition to CD2, PSTPIP associated with CD4, CD8, CD54, and CD62L. CD2 and CD4 ligation reciprocally regulated their association with PSTPIP. These findings indicate that T cell activation, particularly through the CD3 and CD28 signal transduction pathways, regulates PSTPIP-CD2 interactions. PSTPIP likely has additional broader effects through interactions with CD4, CD8, CD54, and CD62L, and this may influence T cell responses to antigen.
Authors:
Y Bai; Y Ding; S Spencer; L A Lasky; J S Bromberg
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Experimental and molecular pathology     Volume:  71     ISSN:  0014-4800     ISO Abbreviation:  Exp. Mol. Pathol.     Publication Date:  2001 Oct 
Date Detail:
Created Date:  2001-10-15     Completed Date:  2001-12-05     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0370711     Medline TA:  Exp Mol Pathol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  115-24     Citation Subset:  IM    
Copyright Information:
Copyright 2001 Academic Press.
Affiliation:
Institute for Gene Therapy and Molecular Medicine, Mount Sinai School of Medicine, New York, New York 10029-6574, USA.
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MeSH Terms
Descriptor/Qualifier:
Adaptor Proteins, Signal Transducing*
Animals
Antibodies, Monoclonal
Antigens, CD2 / metabolism*
Antigens, CD28 / physiology
Antigens, CD3 / physiology
Blotting, Western
Carrier Proteins / metabolism*
Cytoskeletal Proteins / metabolism*
Female
Lymphocyte Activation*
Mice
Mice, Inbred CBA
Mice, Knockout
Phosphorylation
Precipitin Tests
Protein Tyrosine Phosphatases / pharmacology
Receptors, Antigen, T-Cell / metabolism
T-Lymphocytes / physiology*
Grant Support
ID/Acronym/Agency:
R01 AI41428/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Antibodies, Monoclonal; 0/Antigens, CD2; 0/Antigens, CD28; 0/Antigens, CD3; 0/Carrier Proteins; 0/Cytoskeletal Proteins; 0/Pstpip1 protein, mouse; 0/Receptors, Antigen, T-Cell; EC 3.1.3.48/Protein Tyrosine Phosphatases

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