Document Detail


SPAP2, an Ig family receptor containing both ITIMs and ITAMs.
MedLine Citation:
PMID:  12051764     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
This study reports cloning and characterization of SPAP2, a novel transmembrane protein. The extracellular portion of SPAP2 contains six immunoglobulin-like domains and its intracellular segment has two immunoreceptor tyrosine-based activation motifs (ITAMs) and two immunoreceptor tyrosine-based inhibition motifs (ITIMs). We also identified four alternatively spliced products. Sequence alignment with the genomic database revealed that the SPAP2 gene contains 16 exons and is localized at chromosome 1q21. PCR analyses demonstrated that SPAP2 mRNA is expressed in restricted human tissues including the kidney, salivary gland, adrenal gland, uterus, and bone marrow. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. Finally, recruitment of SHP-1 to the tyrosine-phosphorylated ITIMs led to a marked activation of the enzyme.
Authors:
Ming-jiang Xu; Runxiang Zhao; Hongxi Cao; Zhizhuang Joe Zhao
Related Documents :
19299694 - Cutting edge: dok-1 and dok-2 adaptor molecules are regulated by phosphatidylinositol 5...
11739714 - The epstein-barr virus latent membrane protein 1 putative janus kinase 3 (jak3) binding...
9058724 - A tyrosine-phosphorylated protein of 140 kd is constitutively associated with the phosp...
15269224 - Regulation of shp-1 tyrosine phosphatase in human platelets by serine phosphorylation a...
16371594 - Function of cgmp-dependent protein kinases as revealed by gene deletion.
15194504 - The two major imatinib resistance mutations e255k and t315i enhance the activity of bcr...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  293     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2002 May 
Date Detail:
Created Date:  2002-06-07     Completed Date:  2002-06-27     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1037-46     Citation Subset:  IM    
Copyright Information:
(c) 2002 Elsevier Science (USA).
Affiliation:
Hematology/Oncology Division, Department of Medicine, Vanderbilt-Ingram Cancer Center, Vanderbilt University, Nashville, TN 37232-6305, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Alternative Splicing
Amino Acid Motifs
Amino Acid Sequence
Base Sequence
Cell Line
Chromosomes, Human, Pair 1
Cloning, Molecular
Humans
Immunoglobulins / chemistry
Molecular Sequence Data
Protein Isoforms / chemistry,  genetics,  metabolism
Protein Tyrosine Phosphatases / chemistry,  metabolism
Protein-Tyrosine Kinases / chemistry,  metabolism
Receptors, Immunologic / chemistry*,  genetics*,  metabolism
Sequence Alignment
Tissue Distribution
src Homology Domains
Grant Support
ID/Acronym/Agency:
CA-68485/CA/NCI NIH HHS; CA75218/CA/NCI NIH HHS; DK15555/DK/NIDDK NIH HHS; HL-57393/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/FCRL3 protein, human; 0/Immunoglobulins; 0/Protein Isoforms; 0/Receptors, Immunologic; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 3.1.3.48/Protein Tyrosine Phosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Ceramide promotes the death of human cervical tumor cells in the absence of biochemical and morpholo...
Next Document:  Protein Ser/Thr phosphatases PPEF interact with calmodulin.