PU.1 and Spi-B are required for normal B cell receptor-mediated signal transduction. Immunity 1999 Apr;10(4):399-408
Date
05/06/1999Pubmed ID
10229183DOI
10.1016/s1074-7613(00)80040-0Scopus ID
2-s2.0-0033118724 (requires institutional sign-in at Scopus site) 96 CitationsAbstract
PU.1 and Spi-B have previously been implicated in the regulation of genes encoding B cell receptor (BCR) signaling components. Spi-B-/- B lymphocytes respond poorly to BCR stimulation; PU.1-/- mice, however, lack B cells, precluding an analysis of BCR responses. We now show that PU.1+/- Spi-B-/- B cells exhibit more extensive defects than Spi-B-/- B cells, indicating that both PU.1 and Spi-B are required for normal BCR signaling. Strikingly, BCR cross-linking results in substantially reduced protein tyrosine phosphorylation in mutant B cells. Further analysis shows that Igalpha is phosphorylated and syk is recruited and becomes phosphorylated but that BLNK and PLCgamma phosphorylation are defective in mutant cells. Our data support the existence of a novel component coupling syk to downstream targets.
Author List
Garrett-Sinha LA, Su GH, Rao S, Kabak S, Hao Z, Clark MR, Simon MCAuthor
Sridhar Rao MD, PhD Associate Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsB-Lymphocytes
Calcium Signaling
Cell Lineage
Crosses, Genetic
DNA-Binding Proteins
Hematopoietic Stem Cells
Interferon Regulatory Factors
Mice
Mice, Knockout
Phosphorylation
Receptors, Antigen, B-Cell
Signal Transduction
Trans-Activators
Transcription Factors
Tyrosine
