Plant and yeast cornichon possess a conserved acidic motif required for correct targeting of plasma membrane cargos

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F17%3A00477231" target="_blank" >RIV/67985823:_____/17:00477231 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bbamcr.2017.07.004" target="_blank" >http://dx.doi.org/10.1016/j.bbamcr.2017.07.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbamcr.2017.07.004" target="_blank" >10.1016/j.bbamcr.2017.07.004</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Plant and yeast cornichon possess a conserved acidic motif required for correct targeting of plasma membrane cargos

Popis výsledku v původním jazyce

The export of membrane proteins along the secretory pathway is initiated at the endoplasmic reticulum after proteins are folded and packaged inside this organelle by their recruiting into the coat complex COPII vesicles. It is proposed that cargo receptors are required for the correct transport of proteins to its target membrane, however, little is known about ER export signals for cargo receptors. Erv14/Comichon belong to a well conserved protein family in Eukaryotes, and have been proposed to function as cargo receptors for many trans membrane proteins. Amino acid sequence alignment showed the presence of a conserved acidic motif in the C terminal in homologues from plants and yeast. Here, we demonstrate that mutation of the C-terminal acidic motif from ScErv14 or OsCNIH1, did not alter the localization of these cargo receptors, however it modified the proper targeting of the plasma membrane transporters Nhalp, Pdrl2p and Qdr2p. Our results suggest that mistargeting of these plasma membrane proteins is a consequence of a weaker interaction between the cargo receptor and cargo proteins caused by the mutation of the C-terminal acidic motif.

Název v anglickém jazyce

Plant and yeast cornichon possess a conserved acidic motif required for correct targeting of plasma membrane cargos

Popis výsledku anglicky

The export of membrane proteins along the secretory pathway is initiated at the endoplasmic reticulum after proteins are folded and packaged inside this organelle by their recruiting into the coat complex COPII vesicles. It is proposed that cargo receptors are required for the correct transport of proteins to its target membrane, however, little is known about ER export signals for cargo receptors. Erv14/Comichon belong to a well conserved protein family in Eukaryotes, and have been proposed to function as cargo receptors for many trans membrane proteins. Amino acid sequence alignment showed the presence of a conserved acidic motif in the C terminal in homologues from plants and yeast. Here, we demonstrate that mutation of the C-terminal acidic motif from ScErv14 or OsCNIH1, did not alter the localization of these cargo receptors, however it modified the proper targeting of the plasma membrane transporters Nhalp, Pdrl2p and Qdr2p. Our results suggest that mistargeting of these plasma membrane proteins is a consequence of a weaker interaction between the cargo receptor and cargo proteins caused by the mutation of the C-terminal acidic motif.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

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

2017

Kód důvěrnosti údajů

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

Název periodika

Biochimica Et Biophysica Acta-Molecular Cell Research

ISSN

0167-4889

e-ISSN

—

Svazek periodika

1864

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

1809-1818

Kód UT WoS článku

000411168100024

EID výsledku v databázi Scopus

2-s2.0-85025624436