| Literature DB >> 25419229 |
Karthik Krishnan1, David S Askew1.
Abstract
The gateway to the secretory pathway is the endoplasmic reticulum (ER), an organelle that is responsible for the accurate folding, post-translational modification and final assembly of up to a third of the cellular proteome. When secretion levels are high, errors in protein biogenesis can lead to the accumulation of abnormally folded proteins, which threaten ER homeostasis. The unfolded protein response (UPR) is an adaptive signaling pathway that counters a buildup in misfolded and unfolded proteins by increasing the expression of genes that support ER protein folding capacity. Fungi, like other eukaryotic cells that are specialized for secretion, rely upon the UPR to buffer ER stress caused by fluctuations in secretory demand. However, emerging evidence is also implicating the UPR as a central regulator of fungal pathogenesis. In this review, we discuss how diverse fungal pathogens have adapted ER stress response pathways to support the expression of virulence-related traits that are necessary in the host environment.Entities:
Keywords: ER stress; Hac1; HacA; Ire1; IreA; UPR; fungal pathogenesis; fungal virulence; unfolded protein response
Year: 2014 PMID: 25419229 PMCID: PMC4235150 DOI: 10.1016/j.fbr.2014.07.001
Source DB: PubMed Journal: Fungal Biol Rev ISSN: 1749-4613 Impact factor: 4.706