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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Immunoglobulin superfamily, member 8

EWI-2, PGRL, CD316, Estm34
This gene encodes a member the EWI subfamily of the immunoglobulin protein superfamily. Members of this family contain a single transmembrane domain, an EWI (Glu-Trp-Ile)-motif and a variable number of immunoglobulin domains. This protein interacts with the tetraspanins CD81 and CD9 and may regulate their role in certain cellular functions including cell migration and viral infection. The encoded protein may also function as a tumor suppressor by inhibiting the proliferation of certain cancers. Alternate splicing results in multiple transcript variants that encode the same protein. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: Tetraspanin, CD81, FPRP, fibrillin-1, CAN
Papers on EWI-2
EWI-2 negatively regulates TGF-β signaling leading to altered melanoma growth and metastasis.
Hemler et al., Boston, United States. In Cell Res, Mar 2015
In parallel with these "present-absent-present" TGF-β signaling phases, cell surface protein EWI motif-containing protein 2 (EWI-2 or IgSF8) is "absent-present-absent" in melanocytes, primary melanoma, and metastatic melanoma, respectively, suggesting that EWI-2 may serve as a negative regulator of TGF-β signaling.
Complex N-linked glycans serve as a determinant for exosome/microvesicle cargo recruitment.
Mahal et al., New York City, United States. In J Biol Chem, 2014
Furthermore, we show that genetic manipulation of the glycosylation levels of a specific EMV glycoprotein, EWI-2, directly impacts its recruitment as a function of N-linked glycan sites.
Viruses and tetraspanins: lessons from single molecule approaches.
Milhiet et al., Montpellier, France. In Viruses, 2014
In this review we summarize the main results emphasizing the relationship in terms of membrane partitioning between tetraspanins, some of their partners such as Claudin-1 and EWI-2, and viral proteins during infection.
Tetraspanins are involved in Schwann cell-axon interaction.
Carey et al., United States. In J Neurosci Res, 2013
Expression of five of them, CD9, CD63, CD81, CD82, and CD151, and of tetraspanin-associated protein EWI-2 was also confirmed by immunofluorescence.
The tetraspanin network modulates MT1-MMP cell surface trafficking.
Ludwig et al., Heidelberg, Germany. In Int J Biochem Cell Biol, 2013
In short, we found MT1-MMP to interact with the tetraspanin-associated EWI-2 protein by a yeast two-hybrid screen.
Hepatitis C virus entry: role of host and viral factors.
Jahan et al., Lahore, Pakistan. In Infect Genet Evol, 2012
Besides these the expression of certain other conditions such as polarization and EWI-2 expression inhibits the viral cell entry.
Tetraspanin-interacting protein IGSF8 is dispensable for mouse fertility.
Okabe et al., Suita, Japan. In Fertil Steril, 2012
Igsf8-deficient eggs retain the normal level and localization of CD9, resulting in normal microvilli formation indicating that IGSF8 is dispensable in fertility.
EWI-2 association with α-actinin regulates T cell immune synapses and HIV viral infection.
Yáñez-Mó et al., Madrid, Spain. In J Immunol, 2012
The EWI-2/alpha-actinin complex is involved in regulation of the actin cytoskeleton at T cell immune and virological synapses, providing a link between membrane microdomains and the formation of polarized membrane structures involved in T cell recognition.
IgSF8: a developmentally and functionally regulated cell adhesion molecule in olfactory sensory neuron axons and synapses.
Treloar et al., New Haven, United States. In Mol Cell Neurosci, 2012
IgSF8 is present in developing olfactory sensory neuron synapses, and it interacts with Tspan CD9.
Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
Bahn et al., Cambridge, United Kingdom. In J Proteome Res, 2012
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
The thylakoid membrane proteome of two marine diatoms outlines both diatom-specific and species-specific features of the photosynthetic machinery.
Aro et al., Turku, Finland. In J Proteome Res, 2012
PGR5/PGRL homologues were found to be the only protein components of PS I-mediated cyclic electron transport common to both species.
Differential functions of phospholipid binding and palmitoylation of tumour suppressor EWI2/PGRL.
Zhang et al., Memphis, United States. In Biochem J, 2011
This study showed that the EWI2 cytoplasmic tail actively engages with the cell membrane via phosphatidylinositol phosphate binding and palmitoylation.
Interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infection.
Cocquerel et al., Lille, France. In J Biol Chem, 2011
analysis of interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infection
Functional and biochemical studies of CD9 in fibrosarcoma cell line.
Jing et al., Beijing, China. In Mol Cell Biochem, 2011
CD9 overexpression did not affect the expression of TGFα, EGFR, β1, and EWI-2, but EWI-F expression was up-regulated.
Tetraspanin protein contributions to cancer.
Hemler et al., Boston, United States. In Biochem Soc Trans, 2011
Major CD9 partner proteins, such as EWI-2 and EWI-F, may modulate these tumour-suppressor functions.
The cell surface proteome of human mesenchymal stromal cells.
Hoflack et al., Dresden, Germany. In Plos One, 2010
In total 41 CD markers including 5 novel ones (CD97, CD112, CD239, CD276, and CD316) were identified.
The Ig domain protein CD9P-1 down-regulates CD81 ability to support Plasmodium yoelii infection.
Silvie et al., Villejuif, France. In J Biol Chem, 2009
In this study, we investigated the role of the two major molecular partners of CD81 in hepatocytic cells, CD9P-1/EWI-F and EWI-2, two transmembrane proteins belonging to a novel subfamily of immunoglobulin proteins.
Tetraspanins connect several types of Ig proteins: IgM is a novel component of the tetraspanin web on B-lymphoid cells.
Rubinstein et al., Villejuif, France. In Cancer Immunol Immunother, 2004
Thus, tetraspanins may connect several types of proteins with Ig domains, including HLA-DR, EWI-2, and IgM, that may play a role in immune responses.
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