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Identification of rice cornichon as a possible cargo receptor for the Golgi-localized sodium transporter OsHKT1;3
P. Rosas-Santiago, D. Lagunas-Gómez, BJ. Barkla, R. Vera-Estrella, S. Lalonde, A. Jones, WB. Frommer, O. Zimmermannova, H. Sychrová, O. Pantoja,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1996 do Před 1 rokem
Open Access Digital Library
od 1996-01-01
PubMed
25750424
DOI
10.1093/jxb/erv069
Knihovny.cz E-zdroje
- MeSH
- biologický transport MeSH
- endoplazmatické retikulum metabolismus MeSH
- Golgiho aparát metabolismus MeSH
- mapování interakce mezi proteiny MeSH
- membránové transportní proteiny genetika metabolismus fyziologie MeSH
- molekulární sekvence - údaje MeSH
- proteiny přenášející kationty genetika metabolismus MeSH
- rostlinné proteiny genetika metabolismus fyziologie MeSH
- rýže (rod) genetika metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční analýza proteinů MeSH
- sekvenční seřazení MeSH
- sodík metabolismus MeSH
- Xenopus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Membrane proteins are synthesized and folded in the endoplasmic reticulum (ER), and continue their path to their site of residence along the secretory pathway. The COPII system has been identified as a key player for selecting and directing the fate of membrane and secretory cargo proteins. Selection of cargo proteins within the COPII vesicles is achieved by cargo receptors. The cornichon cargo receptor belongs to a conserved protein family found in eukaryotes that has been demonstrated to participate in the selection of integral membrane proteins as cargo for their correct targeting. Here it is demonstrated at the cellular level that rice cornichon OsCNIH1 interacts with OsHKT1;3 and, in yeast cells, enables the expression of the sodium transporter to the Golgi apparatus. Physical and functional HKT-cornichon interactions are confirmed by the mating-based split ubiquitin system, bimolecular fluorescence complementation, and Xenopus oocyte and yeast expression systems. The interaction between the two proteins occurs in the ER of plant cells and their co-expression in oocytes leads to the sequestration of the transporter in the ER. In the yeast cornichon mutant erv14, OsHKT1;3 is mistargeted, preventing the toxic effects of sodium transport in the cell observed in wild-type cells or in the erv14 mutant that co-expressed OsHKT1;3 with either OsCNIH1 or Erv14p. Identification and characterization of rice cornichon as a possible cargo receptor opens up the opportunity to improve our knowledge on membrane protein targeting in plant cells.
Department of Plant Biology Carnegie Institution for Science Stanford CA 94305 USA
Southern Cross Plant Science Southern Cross University Lismore Australia
Citace poskytuje Crossref.org
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