Inhibitory signaling by B cell Fc gamma RIIb (Q28274598)

Current Opinion in Immunology

Europe PubMed Central

title

Inhibitory signaling by B cell Fc gamma RIIb (English)

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author name string

K M Coggeshall

series ordinal

1

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language of work or name

English

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publication date

June 1998

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published in

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volume

10

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issue

3

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page(s)

306-12

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cites work

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Crosslinking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors

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A 13-amino-acid motif in the cytoplasmic domain of FcγRIIB modulates B-cell receptor signalling

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Inhibitory receptors abound?

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ITIMs and ITAMs. The Yin and Yang of antigen and Fc receptor-linked signaling machinery

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The same tyrosine-based inhibition motif, in the intra-cytoplasmic domain of FcγRIIB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation

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Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor

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Recognition and specificity in protein tyrosine kinase-mediated signalling

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Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1.

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Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions

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Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB.

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The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase

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Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2

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The SHIP phosphatase becomes associated with Fc gammaRIIB1 and is tyrosine phosphorylated during 'negative' signaling

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Co-ligation of the antigen and Fc receptors gives rise to the selective modulation of intracellular signaling in B cells. Regulation of the association of phosphatidylinositol 3-kinase and inositol 5'-phosphatase with the antigen receptor complex

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Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif

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Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes

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The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis

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Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP

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Negative signaling via FcgammaRIIB1 in B cells blocks phospholipase Cgamma2 tyrosine phosphorylation but not Syk or Lyn activation

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Fc gammaRIIB1 inhibition of BCR-mediated phosphoinositide hydrolysis and Ca2+ mobilization is integrated by CD19 dephosphorylation

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Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling

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Protein-tyrosine phosphatase SHP-1 is dispensable for FcgammaRIIB-mediated inhibition of B cell antigen receptor activation

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Negative signaling pathways of the killer cell inhibitory receptor and Fc gamma RIIb1 require distinct phosphatases.

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Negative signaling in B cells: SHIP Grbs Shc.

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Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes

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Interaction of Shc with Grb2 regulates the Grb2 association with mSOS

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SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase

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Inositol trisphosphate and calcium signalling

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Inositol 1,3,4,5-tetrakisphosphate activates an endothelial Ca2+-permeable channel

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The function of inositol high polyphosphate binding proteins

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Identification of a specific Ins(1,3,4,5)P4-binding protein as a member of the GAP1 family

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Role of Btk in B cell development and signaling

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The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal.

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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

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Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation

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7 January 2021

Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation

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7 January 2021

Regulation of neuronal survival by the serine-threonine protein kinase Akt

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Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate

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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha

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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B

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PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond

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Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals

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