Tyrosine kinase-dependent ubiquitination of CD16 ζ subunit in human NK cells following receptor engagement

Rossella Paolini, Antonella Serra, Rosa Molfetta, Mario Piccoli, Luigi Frati, Angela Santoni

Research output: Contribution to journalArticle

Abstract

We investigated whether aggregation of the low-affinity immunoglobulin G receptor (CD16) on human NK cells results in receptor ubiquitination. We found that the CD16 ζ subunit becomes ubiquitinated in response to receptor engagement. We then investigated whether protein tyrosine kinase (PTK) activation is required for CD16-mediated receptor ubiquitination. Pretreatment with the PTK inhibitor genistein substantially decreased ligand-induced ζ ubiquitination, suggesting a requirement for PTK activation in receptor ubiquitination. We further analyzed PTK involvement in controlling receptor ubiquitination by using the vaccinia virus expression system. Overexpression of wild-type active lck, but not a kinase-deficient mutant, enhanced both ligand-induced tyrosine phosphorylation and ubiquitination of the CD16 ζ subunit. Taken together, our data demonstrate that CD16 engagement induces ζ chain ubiquitination and strongly suggest a role for lck in regulating this modification.

Original languageEnglish
Pages (from-to)3179-3187
Number of pages9
JournalEuropean Journal of Immunology
Volume29
Issue number10
DOIs
Publication statusPublished - 1999

Keywords

  • Fc receptor
  • NK cell
  • Phosphorylation
  • Signal transduction
  • Ubiquitination

ASJC Scopus subject areas

  • Immunology

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