Ntal/Lab/Lat2

Iwaki, Shoko; Jensen, Bettina M.; Gilfillan, Alasdair M.

doi:10.1016/j.biocel.2006.10.018

Cited by 24 publications

(25 citation statements)

References 16 publications

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“…SH2 domain containing leukocyte protein of 76 kDa is needed for FcgR-mediated ROS production in neutrophils (13), but not in macrophages (14,15), which may be because of differential FcgR expression. Linker for activation of T cells (LAT) and LAT2 can be phosphorylated by Syk and Src kinase Lyn (16,17) and have been shown to be critically involved in myeloid ITAM signaling (18)(19)(20). It has been suggested that FcgRI, but not FcgRIIa, cross-linking leads to phosphorylation of LAT2 in the human monocytic cell line THP-1.…”

Section: Fcgri Downstream Signalingmentioning

confidence: 99%

Functional Characteristics of the High Affinity IgG Receptor, FcγRI

Poel¹,

Spaapen

Winkel

et al. 2011

The Journal of Immunology

150

114

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IgG FcRs are important mediators of immunity and play a key role during Ab-based immunotherapy. Within the leukocyte IgG receptor family, only FcγRI is capable of IgG binding with high affinity. FcγRI exists as a complex of a ligand binding α-chain and an FcR γ-chain. The receptors’ α-chain can, furthermore, elicit several functions independent of the ITAM-bearing FcR γ-chain. Functional implications of high-affinity IgG binding and mechanisms underlying FcR γ-chain–independent signaling remain unclear to this day. In this paper, we provide an overview of past literature on FcγRI and address the implications of recently described interactions between cytosolic proteins and the FcγRI α-chain, as well as cytokine-enhanced FcγRI immune complex binding. Furthermore, an analysis of potential polymorphisms within the FCGR1A gene is provided.

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Section: Fcgri Downstream Signalingmentioning

confidence: 99%

Functional Characteristics of the High Affinity IgG Receptor, FcγRI

Poel¹,

Spaapen

Winkel

et al. 2011

The Journal of Immunology

150

114

View full text Add to dashboard Cite

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“…LAT2 is a transmembrane adaptor in specific cell types of hematopoietic lineages. Functional studies have indicated that LAT2 plays a putative role as regulator of mast cell activation, but its defined role in the organism remains unclear [176].…”

Section: The Single Copy Gene Part Of the Wbs Regionmentioning

confidence: 99%

The genomic basis of the Williams – Beuren syndrome

Schubert

2008

Cell. Mol. Life Sci.

213

161

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. The Williams-Beuren syndrome is a genomic disorder (prevalence: 1/7,500 to 1/20,000), caused by a hemizygous contiguous gene deletion on chromosome 7q11.23. Typical symptoms comprise supravalvular aortic stenosis, mental retardation, overfriendliness and visuospatial impairment. The common deletion sizes range of 1.5–1.8 mega base pairs (Mb), encompassing app. 28 genes. For a few genes, a genotype-phenotype correlation has been established. The best-explored gene within this region is the elastin gene; its haploinsufficiency causes arterial stenosis. The region of the Williams-Beuren syndrome consists of a single copy gene region (~1.2 Mb) flanked by repetitive sequences – Low Copy Repeats (LCR). The deletions arise as a consequence of misalignment of these repetitive sequences during meiosis and a following unequal crossing over due to high similarity of LCRs. This review presents an overview of the Williams-Beuren syndrome region considering the genomic assembly, chromosomal rearrangements and their mechanisms (i.e. deletions, duplications, inversions) and evolutionary and historical aspects.

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“…Cbl proteins containing several protein modulatory regions and most notably a ring finger domain that functions as an E3 ligase in the ubiquitation and rapid down-regulation of various receptors including the EGF, PDGF, T and B cell receptors [82][83][84][85]. However, the insulin receptor does not undergo a rapid down-regulation process following ligand engagement in contrast to these other receptors.…”

Section: Insulin Signaling Leading To Glut4 Translocationmentioning

confidence: 99%

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

132

116

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SummaryGlucose transporter 4 (GLUT4) is the major insulin regulated glucose transporter expressed mainly in muscle and adipose tissue. GLUT4 is stored in a poorly characterized intracellular vesicular compartment and translocates to the cell surface in response to insulin stimulation resulting in increase glucose uptake. This process is essential for the maintenance of normal glucose homeostasis and involves a complex interplay of trafficking events and intracellular signaling cascades. Recent studies have identified sortilin as an essential element for the formation of GLUT4 storage vesicles during adipogenesis and GGA (Golgi-localized γ-ear-containing Arf-binding protein) as a key coat adaptor for the entry of newly synthesized GLUT4 into the specialized compartment. Insulinstimulated GLUT4 translocation from this compartment to the plasma membrane appears to require the Akt/protein kinase B substrate, termed AS160 (Akt Substrate of 160 kDa). In addition, the VPS9 domain-containing protein Gapex-5 in complex with CIP4 appears to function as a Rab31 guanylnucleotide exchange factor that is necessary for insulin-stimulated GLUT4 translocation. Here we attempt to summaries recent advances in GLUT4 vesicle biogenesis, intracellular trafficking and membrane fusion.

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Ntal/Lab/Lat2

Cited by 24 publications

References 16 publications

Functional Characteristics of the High Affinity IgG Receptor, FcγRI

Functional Characteristics of the High Affinity IgG Receptor, FcγRI

The genomic basis of the Williams – Beuren syndrome

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

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