Site-1 protease cleavage site is important for the ER stress-induced activation of membrane-associated transcription factor bZIP28 in Arabidopsis
Cleavage (geology)
ATF6
DOI:
10.1007/s11427-015-4807-6
Publication Date:
2015-01-29T05:14:49Z
AUTHORS (4)
ABSTRACT
Many sources of stress cause accumulation unfolded or misfolded proteins in endoplasmic reticulum (ER), which elicits the protein response (UPR) to either promote cell survival programmed death depending on different developmental context severity. The Arabidopsis membrane-associated transcription factor, bZIP28, is functional equivalent mammalian ATF6, relocates from ER Golgi where it proteolytically processed and released membrane nucleus mediate UPR. Although canonical site-1 protease (S1P) cleavage site lumen-facing domain well conserved between bZIP28 importance S1P has not been experimentally demonstrated. Here we provide genetic evidence that RRIL573 site, but RVLM373 critical for biological function under condition. Further biochemistry biology studies demonstrated required proteolytic processing nuclear relocation stress. Our results reveal plays a pivotal role activation during UPR plants.
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