Expression patterns of genes encoding endomembrane proteins support a reduced function of the Golgi in wheat endosperm during the onset of storage protein deposition

Galia Shy, Linda Ehler, Eliot Herman, Gad Galili

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Wheat storage proteins are deposited in the vacuole of maturing endosperm cells by a novel pathway that is the result of protein body formation by the endoplasmic reticulum followed by autophagy into the central vacuole, bypassing the Golgi apparatus. This model predicts a reduced role of the Golgi in storage protein accumulation, which has been supported by electron microscopy observations. To study this issue further, wheat cDNAs encoding three distinct proteins of the endomembrane system were cloned and characterized. The proteins encoded were homologues (i) of the ER translocon component Sec61α, (ii) the vacuolar sorting receptor BP-80 which is located in the Golgi and clathrin-coated prevacuole vesicles (CCV), and (iii) the Golgi COPI coatomer component COPα. During endosperm development, the levels of all three mRNAs were highest in young stages, before the onset of storage protein synthesis, and declined with seed maturation. However, the relative mRNA levels of BP-80,/Sec61α and the COPα/Sec61α were lower during the onset of storage protein synthesis than at earlier stages of endosperm development. These results support previous studies, suggesting a reduced function of the Golgi apparatus in wheat storage protein transport and deposition.

Original languageEnglish (US)
Pages (from-to)2387-2388
Number of pages2
JournalJournal of Experimental Botany
Volume52
Issue number365
DOIs
StatePublished - Jan 1 2001
Externally publishedYes

Keywords

  • Endomembrane system
  • Endoplasmic reticulum
  • Storage proteins
  • Storage vacuoles
  • Wheat

ASJC Scopus subject areas

  • Physiology
  • Plant Science

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