The SH3-SAM adaptor HACS1 is up-regulated in B cell activation signaling cascades

J Exp Med. 2004 Sep 20;200(6):737-47. doi: 10.1084/jem.20031816.

Abstract

HACS1 is a Src homology 3 and sterile alpha motif domain-containing adaptor that is preferentially expressed in normal hematopoietic tissues and malignancies including myeloid leukemia, lymphoma, and myeloma. Microarray data showed HACS1 expression is up-regulated in activated human B cells treated with interleukin (IL)-4, CD40L, and anti-immunoglobulin (Ig)M and clustered with genes involved in signaling, including TNF receptor-associated protein 1, signaling lymphocytic activation molecule, IL-6, and DEC205. Immunoblot analysis demonstrated that HACS1 is up-regulated by IL-4, IL-13, anti-IgM, and anti-CD40 in human peripheral blood B cells. In murine spleen B cells, Hacs1 can also be up-regulated by lipopolysaccharide but not IL-13. Induction of Hacs1 by IL-4 is dependent on Stat6 signaling and can also be impaired by inhibitors of phosphatidylinositol 3-kinase, protein kinase C, and nuclear factor kappaB. HACS1 associates with tyrosine-phosphorylated proteins after B cell activation and binds in vitro to the inhibitory molecule paired Ig-like receptor B. Overexpression of HACS1 in murine spleen B cells resulted in a down-regulation of the activation marker CD23 and enhancement of CD138 expression, IgM secretion, and Xbp-1 expression. Knock down of HACS1 in a human B lymphoma cell line by small interfering ribonucleic acid did not significantly change IL-4-stimulated B cell proliferation. Our study demonstrates that HACS1 is up-regulated by B cell activation signals and is a participant in B cell activation and differentiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Vesicular Transport / genetics*
  • Adaptor Proteins, Vesicular Transport / physiology
  • Animals
  • B-Lymphocytes / metabolism*
  • Cell Differentiation
  • Gene Expression Regulation*
  • Humans
  • Interleukin-4 / pharmacology
  • Lymphocyte Activation*
  • Mice
  • NF-kappa B / metabolism
  • Phosphatidylinositol 3-Kinases / physiology
  • Phosphorylation
  • Protein Kinase C / physiology
  • STAT6 Transcription Factor
  • Signal Transduction / physiology*
  • Trans-Activators / physiology
  • Tyrosine / metabolism
  • Up-Regulation

Substances

  • Adaptor Proteins, Vesicular Transport
  • NF-kappa B
  • SAMSN1 protein, human
  • SLy2 protein, mouse
  • STAT6 Transcription Factor
  • STAT6 protein, human
  • Stat6 protein, mouse
  • Trans-Activators
  • Interleukin-4
  • Tyrosine
  • Phosphatidylinositol 3-Kinases
  • Protein Kinase C