| Literature DB >> 27943485 |
Evan Angelos1, Cristina Ruberti1, Sang-Jin Kim1,2, Federica Brandizzi1,2,3.
Abstract
Much like a factory, the endoplasmic reticulum (ER) assembles simple cellular building blocks into complex molecular machines known as proteins. In order to protect the delicate protein folding process and ensure the proper cellular delivery of protein products under environmental stresses, eukaryotes have evolved a set of signaling mechanisms known as the unfolded protein response (UPR) to increase the folding capacity of the ER. This process is particularly important in plants, because their sessile nature commands adaptation for survival rather than escape from stress. As such, plants make special use of the UPR, and evidence indicates that the master regulators and downstream effectors of the UPR have distinct roles in mediating cellular processes that affect organism growth and development as well as stress responses. In this review we outline recent developments in this field that support a strong relevance of the UPR to many areas of plant life.Entities:
Keywords: zzm321990Arabidopsis thalianazzm321990; ER stress; IRE1; bZIP28; bZIP60; unfolded protein response
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Year: 2017 PMID: 27943485 PMCID: PMC5415411 DOI: 10.1111/tpj.13449
Source DB: PubMed Journal: Plant J ISSN: 0960-7412 Impact factor: 6.417