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    Keywords: CELLS ; CELL ; MODEL ; SUPPORT ; NEW-YORK ; SITE ; SITES ; PROTEIN ; RESPONSES ; SIMULATION ; BIOLOGY ; MOLECULAR-BIOLOGY ; SIGNAL ; ALPHA ; NUMBER ; FUSION ; EFFICIENT ; OVEREXPRESSION ; ORGANIZATION ; ENDOPLASMIC-RETICULUM ; molecular biology ; molecular ; INCREASE ; COPII ; LEVEL ; endoplasmic reticulum ; EVENTS ; USA ; BIOGENESIS ; INCREASES ; SECRETORY PATHWAY ; CELL BIOLOGY ; PROTEIN-1 ; BREFELDIN-A ; COPII COAT ; DE-NOVO FORMATION ; ER EXPORT ; GOLGI PROTEINS ; phosphatidylinositol-4 kinase III alpha ; Sec16 ; unfolded protein response ; XBP1
    Abstract: The biogenesis of endoplasmic reticulum (ER) exit sites (ERES) involves the formation of phosphatidylinositol-4 phosphate (PI4) and Sec16, but it is entirely unknown how ERES adapt to variations in cargo load. Here, we studied acute and chronic adaptive responses of ERES to an increase in cargo load for ER export. The acute response (within minutes) to increased cargo load stimulated ERES fusion events, leading to larger but less ERES. Silencing either PI4-kinase III alpha (PI4K-III alpha) or Sec16 inhibited the acute response. Overexpression of secretory cargo for 24 h induced the unfolded protein response (UPR), upregulated COPII, and the cells formed more ERES. This chronic response was insensitive to silencing PI4K-III alpha, but was abrogated by silencing Sec16. The UPR was required as the chronic response was absent in cells lacking inositol-requiring protein 1. Mathematical model simulations further support the notion that increasing ERES number together with COPII levels is an efficient way to enhance the secretory flux. These results indicate that chronic and acute increases in cargo load are handled differentially by ERES and are regulated by different factors
    Type of Publication: Journal article published
    PubMed ID: 18650939
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