Literature DB >> 9123836

High concentration of the EBV latent membrane protein 1 in glycosphingolipid-rich complexes from both epithelial and lymphoid cells.

B Clausse1, K Fizazi, V Walczak, C Tetaud, J Wiels, T Tursz, P Busson.   

Abstract

Latent Membrane Protein 1 (LMP1) is an EBV-transforming protein which is detected both in lymphoblastoid cell lines-resulting from EBV-immortalization in vitro- and in undifferentiated nasopharyngeal carcinoma (NPC), an EBV-associated malignancy of epithelial origin. To better define LMP1 subcellular targets, LMP1 distribution was analyzed in cellular glycosphingolipid-rich complexes (GSL-complexes) derived from epithelial and lymphoid cells. These complexes are obtained by extraction of glycosphingolipid-rich membrane domains (GSL-domains), which are clustering sites for heterotrimeric G-proteins and G-protein-associated receptors. LMP1 concentration was enriched 50-fold in GSL-complexes extracted from a NPC tumor line, C15. High concentrations of LMP1 were also observed in GSL-complexes derived from cultured lymphoid and epithelial cells. These data suggest that association with GSL-domains is an important step in LMP1 trafficking and is probably required for some aspects of its biological activity.

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Year:  1997        PMID: 9123836     DOI: 10.1006/viro.1996.8380

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  18 in total

Review 1.  Signaling through sphingolipid microdomains of the plasma membrane: the concept of signaling platform.

Authors:  D C Hoessli; S Ilangumaran; A Soltermann; P J Robinson; B Borisch
Journal:  Glycoconj J       Date:  2000 Mar-Apr       Impact factor: 2.916

2.  C-terminal domain of the Epstein-Barr virus LMP2A membrane protein contains a clustering signal.

Authors:  L Matskova; I Ernberg; T Pawson; G Winberg
Journal:  J Virol       Date:  2001-11       Impact factor: 5.103

3.  CD40 and LMP-1 both signal from lipid rafts but LMP-1 assembles a distinct, more efficient signaling complex.

Authors:  A Kaykas; K Worringer; B Sugden
Journal:  EMBO J       Date:  2001-06-01       Impact factor: 11.598

4.  Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis.

Authors:  William F Coffin; Timothy R Geiger; Jennifer M Martin
Journal:  J Virol       Date:  2003-03       Impact factor: 5.103

5.  A membrane leucine heptad contributes to trafficking, signaling, and transformation by latent membrane protein 1.

Authors:  Jisook Lee; Bill Sugden
Journal:  J Virol       Date:  2007-06-20       Impact factor: 5.103

6.  Glycosylation-related genes are variably expressed depending on the differentiation state of a bioaminergic neuronal cell line: implication for the cellular prion protein.

Authors:  Myriam Ermonval; Daniel Petit; Aurélien Le Duc; Odile Kellermann; Paul-François Gallet
Journal:  Glycoconj J       Date:  2008-10-21       Impact factor: 2.916

7.  Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: protein 1 binds to the cytoskeleton through TNF receptor cytoplasmic factors.

Authors:  M Higuchi; K M Izumi; E Kieff
Journal:  Proc Natl Acad Sci U S A       Date:  2001-04-10       Impact factor: 11.205

8.  High molecular weight complex analysis of Epstein-Barr virus Latent Membrane Protein 1 (LMP-1): structural insights into LMP-1's homo-oligomerization and lipid raft association.

Authors:  Christopher M Wrobel; Timothy R Geiger; Rebecca N Nix; Aaron M Robitaille; Sandra Weigand; Alfredo Cervantes; Miguel Gonzalez; Jennifer M Martin
Journal:  Virus Res       Date:  2013-09-25       Impact factor: 3.303

9.  LMP1 transmembrane domain 1 and 2 (TM1-2) FWLY mediates intermolecular interactions with TM3-6 to activate NF-kappaB.

Authors:  Vishal Soni; Teruhito Yasui; Ellen Cahir-McFarland; Elliott Kieff
Journal:  J Virol       Date:  2006-08-23       Impact factor: 5.103

10.  The cellular prion protein interacts with the tissue non-specific alkaline phosphatase in membrane microdomains of bioaminergic neuronal cells.

Authors:  Myriam Ermonval; Anne Baudry; Florence Baychelier; Elodie Pradines; Mathéa Pietri; Kimimitsu Oda; Benoît Schneider; Sophie Mouillet-Richard; Jean-Marie Launay; Odile Kellermann
Journal:  PLoS One       Date:  2009-08-04       Impact factor: 3.240

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