The B-lymphoid Grb2 interaction code
Konstantin Neumann,
Thomas Oellerich,
Henning Urlaub,
Jürgen Wienands,
Konstantin Neumann
Institute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Search for more papers by this authorThomas Oellerich
Institute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Search for more papers by this authorHenning Urlaub
Max Planck Institute of Biophysical Chemistry, Bioanalytical Mass Spectrometry Group, Göttingen, Germany.
Search for more papers by this authorJürgen Wienands
Institute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Search for more papers by this authorKonstantin Neumann,
Thomas Oellerich,
Henning Urlaub,
Jürgen Wienands,
Konstantin Neumann
Institute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Search for more papers by this authorThomas Oellerich
Institute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Search for more papers by this authorHenning Urlaub
Max Planck Institute of Biophysical Chemistry, Bioanalytical Mass Spectrometry Group, Göttingen, Germany.
Search for more papers by this authorJürgen Wienands
Institute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Search for more papers by this authorJürgen Wienands
Georg August University of GöttingenInstitute of Cellular and Molecular ImmunologyHumboldtallee 34, 37073 Göttingen, GermanyTel.: +49 0551 39 5812Fax: +49 0551 39 5843e-mail: [email protected]
Abstract
Summary: The growth factor receptor-bound protein 2 (Grb2) is a ubiquitously expressed and evolutionary conserved adapter protein possessing a plethora of described interaction partners for the regulation of signal transduction. In B lymphocytes, the Grb2-mediated scaffolding function controls the assembly and subcellular targeting of activating as well as inhibitory signalosomes in response to ligation of the antigen receptor. Also, integration of simultaneous signals from B-cell coreceptors that amplify or attenuate antigen receptor signal output relies on Grb2. Hence, Grb2 is an essential signal integrator. The key question remains, however, of how pathway specificity can be maintained during signal homeostasis critically required for the balance between immune cell activation and tolerance induction. Here, we summarize the molecular network of Grb2 in B cells and introduce a proteomic approach to elucidate the interactome of Grb2 in vivo.
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