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Assembly of the CD8alpha/p56(lck) protein complex in stably expressing rat epithelial cells.

Authors: Pascale, MC  Remondelli, P  Leone, A  Bonatti, S 
Citation: Pascale MC, etal., FEBS Lett. 2000 Sep 1;480(2-3):226-30.
Pubmed: (View Article at PubMed) PMID:11034334

We have previously characterized the biogenesis of the human CD8alpha protein expressed in rat epithelial cells. We now describe the biosynthesis, post-translational maturation and hetero-oligomeric assembly of the human CD8alpha/p56(lck) protein complex in stable transfectants obtained from the same cell line. There were no differences in the myristilation of p56(lck), or in the dimerization, O-glycosylation and transport to the plasma membrane of CD8alpha, between cells expressing either one or both proteins. In the doubly expressing cells, dimeric forms of CD8alpha established hetero-oligomeric complexes with p56(lck), as revealed by co-immunoprecipitation assays performed with anti-CD8alpha antibody. Moreover, p56(lck) bound in these hetero-oligomeric complexes was endowed with auto- and hetero-phosphorylating activity. The present study shows that: (1) the newly synthesized p56(lck) binds rapidly to CD8alpha and most of the p56(lck) is bound to CD8alpha at steady state; (2) CD8alpha/p56(lck) protein complexes are formed at internal membranes as well as at the plasma membrane; and (3) about 50% of complexed p56(lck) reaches the cell surface.

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CRRD Object Information
CRRD ID: 1600230
Created: 2007-03-05
Species: All species
Last Modified: 2007-03-05
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.