The NAC domain-containing protein, GmNAC6, is a downstream component of the ER stress- and osmotic stress-induced NRP-mediated cell-death signaling pathway

January 2011
BMC Plant Biology;2011, Vol. 11 Issue 1, p129
Academic Journal
The article offers information on the study conducted by the authors related to the NAC domain-containing protein, GmNAC6, is a downstream component of the endoplasmic reticulum (ER) stress and osmotic stress-induced NRP-mediated cell-death signaling pathway. It states that the ER is a major signaling organelle, which integrates a variety of responses against physiological stresses.


Related Articles

  • Apoptosis: Managing stress. Smallridge, Rachel // Nature Reviews Molecular Cell Biology;Oct2004, Vol. 5 Issue 10, p772 

    Discusses research being done on the mechanisms that control the apoptotic process linked to stress in the endoplasmic reticulum. Reference to a study by John Reed, et al, which appeared in "Molecular Cell Biology"; Mechanism of action of mammalian Bax inhibitor-1 (BI-1), a known anti-apoptotic...

  • p73-alpha is capable of inducing scotin and ER stress. Terrinoni, Alessandro; Ranalli, Marco; Cadot, Bruno; Leta, Aida; Bagetta, Giacinto; Vousden, Karen H.; Melino, Gerry // Oncogene;4/29/2004, Vol. 23 Issue 20, p3721 

    p73, like its family member p53, can induce programmed cell death following DNA damage. Here, we report that this mechanism also involves endoplasmic reticulum (ER) stress and the transactivation of scotin, a protein identified recently as a p53 target able to induce ER stress. By using Tet-On...

  • GRP94 reduces cell death in SH-SY5Y cells perturbated calcium homeostasis. Bando, Y.; Katayama, T.; Aleshin, A. N.; Manabe, T.; Tohyama, M. // Apoptosis;Jul2004, Vol. 9 Issue 4, p501 

    The endoplasmic reticulum (ER) resident—94 kDa glucose-regulated protein (GRP94), plays a pivotal role in cell death due to ER stress. In our study expression of GRP94 was increased in human neuroblastoma SH-SY5Y cells due to exposure to calcium ionophore A23187. A23187-mediated cell...

  • Interleukin-1 Receptor-Associated Kinase-2 (IRAK2) Is a Critical Mediator of Endoplasmic Reticulum (ER) Stress Signaling Benosman, Samir; Ravanan, Palaniyandi; Correa, Ricardo G.; Hou, Ying-Chen; Yu, Minjia; Gulen, Muhammet Fatih; Li, Xiaoxia; Thomas, James; Cuddy, Michael; Matsuzawa, Yasuko; Sano, Renata; Diaz, Paul; Matsuzawa, Shu-ichi; Reed, John C. // PLoS ONE;May2013, Vol. 8 Issue 5, p1 

    Endoplasmic reticulum (ER) stress occurs when unfolded proteins accumulate in the lumen of the organelle, triggering signal transduction events that contribute either to cellular adaptation and recovery or alternatively to cellular dysfunction and death. ER stress has been implicated in numerous...

  • Role of the unfolded protein response in cell death. Kim, R.; Emi, M.; Tanabe, K.; Murakami, S. // Apoptosis;Jan2006, Vol. 11 Issue 1, p5 

    Unfolded protein response (UPR) is an important genomic response to endoplasmic reticulum (ER) stress. The ER chaperones, GRP78 and Gadd153, play critical roles in cell survival or cell death as part of the UPR, which is regulated by three signaling pathways: PERK/ATF4, IRE1/XBP1 and ATF6....

  • Editorial [Hot Topic: Emerging Roles of the Unfolded Protein Response Signaling in Physiology and Disease (Executive Editor: Claudio A. Hetz and Claudio Soto )]. Hetz, Claudio A.; Soto, Claudio // Current Molecular Medicine;Feb2006, Vol. 6 Issue 1, p1 

    The viability of a cell strictly depends on the functional and structural integration between different subcellular compartments. At each organelle, different molecular sentinels permanently sense stressful cellular conditions and initiate a complex molecular response. This response aims either...

  • Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data. Lavoie, Christine; Paiement, Jacques // Histochemistry & Cell Biology;Feb2008, Vol. 129 Issue 2, p117 

    The endoplasmic reticulum (ER) is a key organelle of the secretion pathway involved in the synthesis of both proteins and lipids destined for multiple sites within and without the cell. The ER functions to both co- and post-translationally modify newly synthesized proteins and lipids and sort...

  • Organelle-specific, rapid induction of molecular activities and membrane tethering. Komatsu, Toru; Kukelyansky, Igor; McCaffery, J. Michael; Ueno, Tasuku; Varela, Lidenys C.; Inoue, Takanari // Nature Methods;Mar2010, Vol. 7 Issue 3, p206 

    Using new chemically inducible dimerization probes, we generated a system to rapidly target proteins to individual intracellular organelles. Using this system, we activated Ras GTPase at distinct intracellular locations and induced tethering of membranes from two organelles, endoplasmic...

  • STIM1 tracks growing microtubule ends. Jermy, Andrew // Nature Cell Biology;Apr2008, Vol. 10 Issue 4, p384 

    The article reports that a group of researchers have identified an interaction between the endoplasmic reticulum (ER) membrane resident, stromal interaction molecule 1 (ST1M1) and the microtubule plus-end-binding protein EB1. According to the article, the EB1 is required for tip-attachment...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics