The lck tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain.

Abstract:

:The CD4 lymphocyte surface glycoprotein and the lck tyrosine protein kinase p56lck are found as a complex in T lymphocytes. We have defined the domains in both proteins that are responsible for this interaction by coexpressing hybrid and deleted forms of the two proteins in HeLa cells. We have found that the unique 32 amino-terminal residues of p56lck and the 38 carboxy-terminal residues of CD4 that comprise the cytoplasmic domain are both necessary and sufficient by themselves for the interaction of the two proteins. The interaction appears to be independent of other T cell-specific proteins and probably occurs before CD4 reaches the cell surface. Our findings suggest that the specialized amino-terminal domains of other members of the src family of intracellular tyrosine kinases may also mediate transmembrane signaling via coupling to the cytoplasmic domains of specific transmembrane proteins.

journal_name

Cell

journal_title

Cell

authors

Shaw AS,Amrein KE,Hammond C,Stern DF,Sefton BM,Rose JK

doi

10.1016/0092-8674(89)90008-1

subject

Has Abstract

pub_date

1989-11-17 00:00:00

pages

627-36

issue

4

eissn

0092-8674

issn

1097-4172

pii

0092-8674(89)90008-1

journal_volume

59

pub_type

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