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 Cgamma2 (PLCgamma2), which, unlike activation of the migration regulatory GTPases Rac or Rap1, was mediated by Btk. PLCgamma2-deficient B cells also exhibited impaired SDF-1-controlled migration. These results reveal that Btk and PLCgamma2 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).
journal_name
Immunityjournal_title
Immunityauthors
de Gorter DJ,Beuling EA,Kersseboom R,Middendorp S,van Gils JM,Hendriks RW,Pals ST,Spaargaren Mdoi
10.1016/j.immuni.2006.11.012subject
Has Abstractpub_date
2007-01-01 00:00:00pages
93-104issue
1eissn
1074-7613issn
1097-4180pii
S1074-7613(06)00568-1journal_volume
26pub_type
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