Assembly of the CD8α/p56 lck protein complex in stably expressing rat epithelial cells
We have previously characterized the biogenesis of the human CD8α protein expressed in rat epithelial cells. We now describe the biosynthesis, post-translational maturation and hetero-oligomeric assembly of the human CD8α/p56 lck protein complex in stable transfectants obtained from the same cell li...
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Published in | FEBS letters Vol. 480; no. 2; pp. 226 - 230 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
01.09.2000
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Subjects | |
Online Access | Get full text |
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Summary: | We have previously characterized the biogenesis of the human CD8α protein expressed in rat epithelial cells. We now describe the biosynthesis, post-translational maturation and hetero-oligomeric assembly of the human CD8α/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 CD8α, between cells expressing either one or both proteins. In the doubly expressing cells, dimeric forms of CD8α established hetero-oligomeric complexes with p56
lck
, as revealed by co-immunoprecipitation assays performed with anti-CD8α 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 CD8α and most of the p56
lck
is bound to CD8α at steady state; (2) CD8α/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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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(00)01945-1 |