Divergent substrate-binding loop within the pro-oncogenic protein anterior gradient-2 forms a docking site for reptin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F10%3A%230000597" target="_blank" >RIV/00209805:_____/10:#0000597 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00209805:_____/10:#0000680

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0022283610010235" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0022283610010235</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jmb.2010.09.035" target="_blank" >10.1016/j.jmb.2010.09.035</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Divergent substrate-binding loop within the pro-oncogenic protein anterior gradient-2 forms a docking site for reptin

Popis výsledku v původním jazyce

Anterior gradient-2 (AGR2) functions in a range of biological systems, including goblet cell formation, limb regeneration, inhibition of p53, and metastasis. There are no well-validated binding proteins for AGR2 protein despite the wealth of data implicating an important cellular function in vertebrates. The yeast two-hybrid system was used to isolate the ATP binding protein Reptin as an AGR2-interacting protein. AGR2 formed a stable complex in human cell lysates with Reptin, thus validating Reptin as an AGR2 binding protein in cells. Reptin was also shown to be overproduced in a panel of primary breast cancer biopsy specimens, relative to normal adjacent tissue from the same patient, suggesting a role in cancer growth in vivo. Mutations were made at the two ATP binding motifs in Reptin to evaluate the effects of ATP on Reptin?AGR2 complex stability. Loss-of-ATP binding mutations at the Walker A motif (K83A) or gain-of- ATP binding mutations at the Walker B motif (D299N) resulted in Re

Název v anglickém jazyce

Divergent substrate-binding loop within the pro-oncogenic protein anterior gradient-2 forms a docking site for reptin

Popis výsledku anglicky

Anterior gradient-2 (AGR2) functions in a range of biological systems, including goblet cell formation, limb regeneration, inhibition of p53, and metastasis. There are no well-validated binding proteins for AGR2 protein despite the wealth of data implicating an important cellular function in vertebrates. The yeast two-hybrid system was used to isolate the ATP binding protein Reptin as an AGR2-interacting protein. AGR2 formed a stable complex in human cell lysates with Reptin, thus validating Reptin as an AGR2 binding protein in cells. Reptin was also shown to be overproduced in a panel of primary breast cancer biopsy specimens, relative to normal adjacent tissue from the same patient, suggesting a role in cancer growth in vivo. Mutations were made at the two ATP binding motifs in Reptin to evaluate the effects of ATP on Reptin?AGR2 complex stability. Loss-of-ATP binding mutations at the Walker A motif (K83A) or gain-of- ATP binding mutations at the Walker B motif (D299N) resulted in Re

Druh

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

CEP obor

EB - Genetika a molekulární biologie

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)

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Journal of molecular biology

ISSN

0022-2836

e-ISSN

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Svazek periodika

404

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

21

Strana od-do

418-438

Kód UT WoS článku

000285372700007

EID výsledku v databázi Scopus

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