Polyomavirus Middle T-Antigen Is a Transmembrane Protein That Binds Signaling Proteins in Discrete Subcellular Membrane Sites

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10106664" target="_blank" >RIV/00216208:11310/11:10106664 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1128/JVI.02209-10" target="_blank" >http://dx.doi.org/10.1128/JVI.02209-10</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/JVI.02209-10" target="_blank" >10.1128/JVI.02209-10</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Polyomavirus Middle T-Antigen Is a Transmembrane Protein That Binds Signaling Proteins in Discrete Subcellular Membrane Sites

Popis výsledku v původním jazyce

Murine polyomavirus middle T-antigen (MT) induces tumors by mimicking an activated growth factor receptor. An essential component of this action is a 22-amino-acid hydrophobic region close to the C terminus which locates MT to cell membranes. Here, we demonstrate that this sequence is a transmembrane domain (TMD) by showing that a hemagglutinin (HA) tag added to the MT C terminus is exposed on the outside of the cells, with the N terminus inside. The mutant protein with addition of the ER retention signal KDEL to the MT C terminus, locates only in the ER, demonstrating that MT does insert into membranes solely at this location. In addition, this ER-located MT failed to transform. MTKDEL protein failed to interact with ShcA, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-1 (PLC-1), despite being tyrosine phosphorylated. Additional studies showed that MT binding to PP2A is probably required for MT to ef?ciently exit the ER and migrate to the plasma membrane. Overall, these dat

Název v anglickém jazyce

Polyomavirus Middle T-Antigen Is a Transmembrane Protein That Binds Signaling Proteins in Discrete Subcellular Membrane Sites

Popis výsledku anglicky

Murine polyomavirus middle T-antigen (MT) induces tumors by mimicking an activated growth factor receptor. An essential component of this action is a 22-amino-acid hydrophobic region close to the C terminus which locates MT to cell membranes. Here, we demonstrate that this sequence is a transmembrane domain (TMD) by showing that a hemagglutinin (HA) tag added to the MT C terminus is exposed on the outside of the cells, with the N terminus inside. The mutant protein with addition of the ER retention signal KDEL to the MT C terminus, locates only in the ER, demonstrating that MT does insert into membranes solely at this location. In addition, this ER-located MT failed to transform. MTKDEL protein failed to interact with ShcA, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-1 (PLC-1), despite being tyrosine phosphorylated. Additional studies showed that MT binding to PP2A is probably required for MT to ef?ciently exit the ER and migrate to the plasma membrane. Overall, these dat

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Virology

ISSN

0022-538X

e-ISSN

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Svazek periodika

85

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

3046-3054

Kód UT WoS článku

000288373000001

EID výsledku v databázi Scopus

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