Faculty Opinions recommendation of Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development.

2002 ◽  
Author(s):  
Mary-Jane Gething
Keyword(s):  
Unfolded Protein Response ◽  
Signaling Pathways ◽  
C Elegans ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Complementary Signaling Pathways Regulate the Unfolded Protein Response and Are Required for C. elegans Development

Cell ◽  
2001 ◽  
Vol 107 (7) ◽  
pp. 893-903 ◽  
Author(s):  
Xiaohua Shen ◽  
Ronald E. Ellis ◽  
Kyungho Lee ◽  
Chuan-Yin Liu ◽  
Kun Yang ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Signaling Pathways ◽  
C Elegans ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals HSP-4/BiP expression in secretory cells is regulated by a lineage-dependent differentiation program and not by the unfolded protein response

2018 ◽  
Author(s):  
Ji Zha ◽  
Jasmine Alexander-Floyd ◽  
Tali Gidalevitz
Keyword(s):  
Unfolded Protein Response ◽  
Secretory Cells ◽  
C Elegans ◽  
Unfolded Protein ◽  
Daughter Cells ◽  
Developmental Program ◽  
The Unfolded Protein Response ◽  
Stress Dependent ◽  
Protein Response ◽  
Anticipatory Activation

AbstractDifferentiation of secretory cells leads to sharp increases in protein synthesis, challenging ER proteostasis. Anticipatory activation of the unfolded protein response (UPR) prepares cells for the onset of secretory function by expanding the ER size and folding capacity. How cells ensure that the repertoire of induced chaperones matches their post-differentiation folding needs is not well understood. We find that during differentiation of stem-like seam cells, a typical UPR target, the C. elegans BiP homologue HSP-4, is selectively induced in alae-secreting daughter cells, but is repressed in hypodermal daughter cells. Surprisingly, this lineage-dependent induction bypasses the requirement for UPR signaling, and instead is controlled by a specific developmental program. The repression of HSP-4 in hypodermal-fated cells requires a transcriptional regulator BLMP-1/BLIMP1, involved in differentiation of mammalian secretory cells. The HSP-4 induction is anticipatory, and is required for the integrity of secreted alae. Thus, differentiation programs can directly control a broad-specificity chaperone that is normally stress-dependent, to ensure the integrity of secreted proteins.

scholarly journals Depletion of the C. elegans NAC Engages the Unfolded Protein Response, Resulting in Increased Chaperone Expression and Apoptosis

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e44038 ◽  
Author(s):  
Paul T. Arsenovic ◽  
Anthony T. Maldonado ◽  
Vaughn D. Colleluori ◽  
Tim A. Bloss
Keyword(s):  
Unfolded Protein Response ◽  
C Elegans ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Modulation of the Unfolded Protein Response by the Severe Acute Respiratory Syndrome Coronavirus Spike Protein

2006 ◽  
Vol 80 (18) ◽  
pp. 9279-9287 ◽  
Author(s):  
Ching-Ping Chan ◽  
Kam-Leung Siu ◽  
King-Tung Chin ◽  
Kwok-Yung Yuen ◽  
Bojian Zheng ◽  
...  
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Unfolded Protein Response ◽  
Signaling Pathways ◽  
Transcriptional Activation ◽  
Cultured Cells ◽  
Protein A ◽  
S Protein ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

ABSTRACT Perturbation of the function of endoplasmic reticulum (ER) causes stress leading to the activation of cell signaling pathways known as the unfolded protein response (UPR). Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) uses ER as a site for synthesis and processing of viral proteins. In this report, we demonstrate that infection with SARS-CoV induces the UPR in cultured cells. A comparison with M, E, and NSP6 proteins indicates that SARS-CoV spike (S) protein sufficiently induces transcriptional activation of several UPR effectors, including glucose-regulated protein 78 (GRP78), GRP94, and C/EBP homologous protein. A substantial amount of S protein accumulates in the ER. The expression of S protein exerts different effects on the three major signaling pathways of the UPR. Particularly, it induces GRP78/94 through PKR-like ER kinase but has no influence on activating transcription factor 6 or X box-binding protein 1. Taken together, our findings suggest that SARS-CoV S protein specifically modulates the UPR to facilitate viral replication.

Sign in / Sign up

Export Citation Format

Share Document