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Literature DB >> 18953613

SH3BP2 is a critical regulator of macrophage and osteoclast response to M-CSF and RANKL stimulation.

Abstract

The protein Src homology 3 domain-binding protein 2 (SH3BP2) is a regulator of tumor necrosis factor (TNF)-alpha generation in macrophages and of osteoclast differentiation. SH3BP2 regulates bone marrow monocyte responses to macrophage and osteoclast differentiation signals downstream of the receptors for macrophage colony-stimulating factor and receptor activator of nuclear factor kappaB ligand. SH3BP2 is a potential target for the development of novel anti-TNF-alpha therapeutic interventions as well as a target for suppression of osteoclastogenesis.

Entities: Gene

Year: 2008 PMID： 18953613 PMCID： PMC2642551 DOI： 10.1007/s11420-008-9091-6

Source DB: PubMed Journal: HSS J ISSN： 1556-3316

12 in total

1. Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause cherubism.

Authors: Y Ueki; V Tiziani; C Santanna; N Fukai; C Maulik; J Garfinkle; C Ninomiya; C doAmaral; H Peters; M Habal; L Rhee-Morris; J B Doss; S Kreiborg; B R Olsen; E Reichenberger
Journal: Nat Genet Date: 2001-06 Impact factor: 38.330

2. The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor.

Authors: Isabelle Foucault; Séverine Le Bras; Céline Charvet; Chéol Moon; Amnon Altman; Marcel Deckert
Journal: Blood Date: 2004-09-02 Impact factor: 22.113

SH3BP2 is a critical regulator of macrophage and osteoclast response to M-CSF and RANKL stimulation.

1. Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause cherubism.

2. The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor.

3. 3BP2 deficiency impairs the response of B cells, but not T cells, to antigen receptor ligation.

4. Adaptor function for the Syk kinases-interacting protein 3BP2 in IL-2 gene activation.

5. Identification of a ten-amino acid proline-rich SH3 binding site.

6. Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase.

7. Abl-SH3 binding protein 2, 3BP2, interacts with CIN85 and HIP-55.

8. TNF-alpha induction by LPS is regulated posttranscriptionally via a Tpl2/ERK-dependent pathway.

9. SH3BP2 is an activator of NFAT activity and osteoclastogenesis.

10. The chaperone protein 14-3-3 interacts with 3BP2/SH3BP2 and regulates its adapter function.

Review 1. Type I interferons and endoplasmic reticulum stress in health and disease.