Bruton's tyrosine kinase and phospholipase C gamma 2 mediate chemokine-controlled B cell migration and homing

David J. J. de Gorter, Esther A. Beuling, Rogier Kersseboom, Sabine Middendorp, Janine M. van Gils, Rudolf W. Hendriks, Steven T. Pals, Marcel Spaargaren

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250 Citations (Scopus)

Abstract

Control of integrin-mediated adhesion and migration by chemokines plays a critical role in B cell development, differentiation, and function; however, the underlying signaling mechanisms are poorly defined. Here we show that the chemokine SDF-1 induced activation of Bruton's tyrosine kinase (Btk) and that integrin-mediated adhesion and migration in response to SDF-1 or CXCL13, as well as in vivo homing to lymphoid organs, was impaired in Btk-deficient (pre-)B cells. Furthermore, SDF-1 induced tyrosine phosphorylation of Phospholipase C gamma 2 (PLC gamma 2), which, unlike activation of the migration regulatory GTPases Rac or Rap1, was mediated by Btk. PLC gamma 2-deficient B cells also exhibited impaired SDF-1-controlled migration. These results reveal that Btk and PLC gamma 2 mediate chemokine-controlled migration, thereby providing insights into the control of B cell homeostasis, trafficking, and function, as well as into the pathogenesis of the immunodeficiency disease X-linked agammaglobulinemia (XLA)
Original languageEnglish
Pages (from-to)93-104
JournalImmunity
Volume26
Issue number1
DOIs
Publication statusPublished - 2007

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