Cross-linking of CD4 induces cytoskeletal association of CD4 and p56(lck)

Young Mie Ha-Lee, Yoonsil Lee, Young Kee Kim, Jeongwon Sohn

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


A membrane glycoprotein CD4 functions as a coreceptor of a T lymphocyte. The co-receptor function has been attributed to a protein tyrosine kinase, p56(lck), which is activated upon CD4 binding to MHC molecule. In this study, we present evidences that one of the pathways through which CD4 transmits its signal is cytoskeleton association of p56(lck) tyrosine kinase as well as CD4 itself. Cytoskeletal association of both proteins is inhibited by a tyrosine kinase inhibitor, genistein, indicating that tyrosine protein kinase activation is important for cytoskeletal association of CD4 and p56(lck). Cytoskeletal association of these proteins by CD4 cross-linking is not affected by inhibitors of protein kinase C nor PI3-kinase. Taken together, these results suggest that CD4 cross-linking activates a tyrosine kinase which then induces the simultaneous association of CD4 and p56(lck) with cytoskeleton.

Original languageEnglish
Pages (from-to)18-22
Number of pages5
JournalExperimental and Molecular Medicine
Issue number1
Publication statusPublished - 2000 Mar 31
Externally publishedYes


  • CD4
  • Ccytoskeletal association
  • P56(lck)
  • T cells
  • Tyrosine kinase inhibition

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry


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