Disease relevance of Fyb

• By using Fyb domains as bait to screen a mouse lymphoma cDNA library, we identified a novel interaction partner, mammalian actin binding protein 1 (mAbp1) [1].
• The immune cell specific protein Fyn-T binding protein (Fyb) has been identified as a target of the Yersinia antiphagocytic effector Yersinia outer protein H (YopH), but its role in macrophages is unknown [1].

Psychiatry related information on Fyb

• The beads were coated with polyclonal IgG purified from sera obtained from rabbits immunized with a highly enriched Alzheimer's disease brain protein fraction for ADAP [2].

High impact information on Fyb

• Coupling of the TCR to integrin activation by Slap-130/Fyb [3].
• In addition, the T cell receptor (TCR) in SLAP-130/Fyb mutant cells fails to enhance integrin-dependent adhesion [3].
• We demonstrate that Fyb/Slap-deficient T cells exhibit defective proliferation and cytokine production in response to TCR stimulation [4].
• ADAP-SLP-76 binding differentially regulates supramolecular activation cluster (SMAC) formation relative to T cell-APC conjugation [5].
• ADAP also colocalized with LFA-1 at the immunological synapse [5].

Chemical compound and disease context of Fyb

• Interaction between the Yersinia tyrosine phosphatase YopH and its macrophage substrate, Fyn-binding protein, Fyb [6].

Biological context of Fyb

• Because they also induce tyrosine phosphorylation of the ADAP adapter, we investigated ADAP's role in GP Ib-IX-V signal transduction [7].
• Thus, failure to bind ADAP does not underlie the functional defects exhibited by SLP-76 SH2 domain mutant-expressing mast cells [8].
• ADAP thus may play an important role as a partner of c-Src for cell migration and progression to the multinucleated cell stage in osteoclastogenesis in vitro [9].
• We suggest that dephosphorylation of SKAP-HOM and Fyb by YopH allows yersiniae to interfere with a novel adhesion-regulated signal transduction pathway in macrophages [10].
• In addition, we obtained evidence that SKAP-HOM is tyrosine phosphorylated in response to macrophage cell adhesion and that it forms a signalling complex with Fyb [10].

Anatomical context of Fyb

• Characterization of signaling molecules such as SLP-76, SLAM, SAP, and Fyb in the mucosal immune system will be an important area of future research [11].
• Previously, several groups have provided experimental evidence that SKAP-HOM (most likely in cooperation with the cytosolic adaptor protein ADAP) is involved in regulating leukocyte adhesion [12].
• Surprisingly, we found that mast cells lacking ADAP expression demonstrate no defects in FcepsilonRI-induced adhesion, granule release, or IL-6 production, and that ADAP-deficient mice produce a normal passive systemic anaphylactic response [8].
• ADAP was found to be expressed in cells at the prefusion stage and localized mainly in the leading edge of lamellipodia and in pseudopodia [9].
• In this study, we searched for c-Src-binding proteins using a combination of pull-down assays and mass spectrometric analysis, and identified the association of adhesion and degranulation promoting adaptor protein (ADAP) with c-Src in RAW264 cells and osteoclast precursors prepared from bone marrow cells [9].

Associations of Fyb with chemical compounds

• By contrast, collagen-induced phosphorylation of the adapter ADAP (adhesion- and degranulation-promoting adapter protein) was substantially potentiated by U46619 to levels equivalent to those observed in wild-type platelets [13].
• Use of the MAIEA assay to demonstrate that Fy3 is on the same glycoprotein as Fy6, Fya, and Fyb [14].
• The phosphotyrosine substrate binding N-terminal part (1-130) of YopH as well as the C-terminal catalytic region binds to Fyb in a phosphotyrosine-dependent manner [6].

Physical interactions of Fyb

• We show that mAbp1 binds the Fyb N-terminal via its C-terminally located src homology 3 domain [1].

Regulatory relationships of Fyb

• Physical and functional association of c-Src and adhesion and degranulation promoting adaptor protein (ADAP) in osteoclastogenesis in vitro [9].

Other interactions of Fyb

• Hence, mAbp1 is likely to constitute a downstream effector of Fyb involved in F-actin dynamics [1].
• This work identifies SLP-76 as an important adapter molecule that is regulated by Syk and lies upstream of SLAP-130 and PLC-gamma2 in CRP-stimulated platelets [15].
• We demonstrate here that two major MIST-associated phosphoproteins expressed in mast cell lines are SLAP-130 and SKAP55, adaptors known to interact with the Src-homology (SH) 2 domain of Src-family protein tyrosine kinases (PTKs) [16].
• MIST directly associated with SLAP-130 via its SH2 domain, and collaboration of SLAP-130 with SKAP55 was required for the recruitment of MIST to Lyn [16].
• Analysis of ligand bound per cell demonstrated no significant difference in binding of erythrocyte antibodies to platelets from donors homozygous, heterozygous, or negative for D, C, c, E, e, Fya, Fyb, Jka, Jkb , K, k, and Lub antigens [17].

References