Limits...
Endoplasmic reticulum-shape and function in stress translation.

Brandizzi F, Frigerio L, Howell SH, Schäfer P - Front Plant Sci (2014)

View Article: PubMed Central - PubMed

Affiliation: Plant Research Laboratory, Department of Energy, Michigan State University East Lansing, MI, USA.

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

The ER is a dynamic network of membrane tubules and sheets... Movement of the ER along the actin cytoskeleton has a significant influence on both its architecture and dynamics... To insure that only correctly folded proteins are exported from the ER, eukaryotes have evolved ER quality control (ERQC) mechanisms, which supervise the folding process... Protein folding is monitored through the stepwise modification of oligosaccharide side chains on glycoproteins, and proteins that fail to fold correctly are extracted from the folding process and subjected to ER associated degradation (ERAD)... Srivastava et al. describe the structure of bZIP28 and underlying principles of bZIP28 mobilization in response to stress... ER stress activates the unfolded proteins response (UPR) and the ERAD system to eliminate misfolded proteins, which is vital for the establishment of an effective immune system... The overall significance of the ER in stress adaption is however apparent and underlined by the review of Nakano et al. which, in addition to the biogenesis and evolution, discusses the putative function of ER bodies in abiotic and biotic stress... As ER-derived compartments ER bodies contain stress-associated proteins (e.g., various β-glucosidases of the PYK10 family) that are thought to enhance stress resilience by activating glucosinolates and glucosylated phytohormones... Cells mount adaptive responses (e.g., UPR) to mitigate the damage caused by ER stress... Williams et al. review the possible links between the UPR and PCD and discuss the involvement of calcium signaling and N-rich proteins in promoting PCD and the role of ER chaperones in limiting it as well as the connection of pathogens to ER-mediated cell death... Cai et al. finally compare the activation and/or regulation of ER stress-induced PCD in animals and plants and highlight the significance of caspase and caspase-like activities in underlying PCD processes... By providing a stable microenvironment for the synthesis of metabolites and secreted proteins, the ER functions as an intracellular stress sensory organelle and, accordingly, initiates and regulates adaptive responses to environmental stress... Understanding the molecular basis of these processes and the role of ER architectural dynamics therein is of high relevance for sustainable crop production... We hope our e-book will stimulate research in the field to further enhance our knowledge of ER biology in plants.

No MeSH data available.


Related in: MedlinePlus

Schematic representation of topics covered in the special issue. Numbers correspond to review articles as follows: (1) Griffing et al. (2014), ER network dynamics are differentially controlled by myosins XI-K, XI-C, XI-E, XI-I, XI-1, and XI-2, (2) Viotti (2014), ER and vacuoles: never been closer, (3) Li and Liu (2014), Endoplasmic reticulum-mediated protein quality control in Arabidopsis, (4) Ruberti and Brandizzi (2014), Conserved and plant-unique strategies for overcoming endoplasmic reticulum stress, (5) Srivastava et al. (2014), Stress sensing in plants by an ER stress sensor/transducer, bZIP28, (6) Tintor and Saijo (2014), ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants, (7) Verchot (2014), The ER quality control and ER associated degradation machineries are vital for viral pathogenesis, (8) Nakano et al. (2014), ER bodies in plants of the Brassicales order: biogenesis and association with innate immunity, (9) Höwing et al. (2014), Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense, (10) Williams et al. (2014), When supply does not meet demand-ER stress and plant programmed cell death, (11) Cai et al. (2014), Endoplasmic reticulum stress-induced PCD and caspase-like activities involved.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4150462&req=5

Figure 1: Schematic representation of topics covered in the special issue. Numbers correspond to review articles as follows: (1) Griffing et al. (2014), ER network dynamics are differentially controlled by myosins XI-K, XI-C, XI-E, XI-I, XI-1, and XI-2, (2) Viotti (2014), ER and vacuoles: never been closer, (3) Li and Liu (2014), Endoplasmic reticulum-mediated protein quality control in Arabidopsis, (4) Ruberti and Brandizzi (2014), Conserved and plant-unique strategies for overcoming endoplasmic reticulum stress, (5) Srivastava et al. (2014), Stress sensing in plants by an ER stress sensor/transducer, bZIP28, (6) Tintor and Saijo (2014), ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants, (7) Verchot (2014), The ER quality control and ER associated degradation machineries are vital for viral pathogenesis, (8) Nakano et al. (2014), ER bodies in plants of the Brassicales order: biogenesis and association with innate immunity, (9) Höwing et al. (2014), Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense, (10) Williams et al. (2014), When supply does not meet demand-ER stress and plant programmed cell death, (11) Cai et al. (2014), Endoplasmic reticulum stress-induced PCD and caspase-like activities involved.

Mentions: The endoplasmic reticulum (ER) is a very versatile organelle. Besides its major role as the gateway to the secretory pathway the ER is central to adaptation against abiotic and biotic stress. Here, we summarize the current knowledge on ER dynamics and architecture, the association and interaction of the ER with other organelles as well as its role in stress translation and adaptation (Figure 1).


Endoplasmic reticulum-shape and function in stress translation.

Brandizzi F, Frigerio L, Howell SH, Schäfer P - Front Plant Sci (2014)

Schematic representation of topics covered in the special issue. Numbers correspond to review articles as follows: (1) Griffing et al. (2014), ER network dynamics are differentially controlled by myosins XI-K, XI-C, XI-E, XI-I, XI-1, and XI-2, (2) Viotti (2014), ER and vacuoles: never been closer, (3) Li and Liu (2014), Endoplasmic reticulum-mediated protein quality control in Arabidopsis, (4) Ruberti and Brandizzi (2014), Conserved and plant-unique strategies for overcoming endoplasmic reticulum stress, (5) Srivastava et al. (2014), Stress sensing in plants by an ER stress sensor/transducer, bZIP28, (6) Tintor and Saijo (2014), ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants, (7) Verchot (2014), The ER quality control and ER associated degradation machineries are vital for viral pathogenesis, (8) Nakano et al. (2014), ER bodies in plants of the Brassicales order: biogenesis and association with innate immunity, (9) Höwing et al. (2014), Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense, (10) Williams et al. (2014), When supply does not meet demand-ER stress and plant programmed cell death, (11) Cai et al. (2014), Endoplasmic reticulum stress-induced PCD and caspase-like activities involved.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4150462&req=5

Figure 1: Schematic representation of topics covered in the special issue. Numbers correspond to review articles as follows: (1) Griffing et al. (2014), ER network dynamics are differentially controlled by myosins XI-K, XI-C, XI-E, XI-I, XI-1, and XI-2, (2) Viotti (2014), ER and vacuoles: never been closer, (3) Li and Liu (2014), Endoplasmic reticulum-mediated protein quality control in Arabidopsis, (4) Ruberti and Brandizzi (2014), Conserved and plant-unique strategies for overcoming endoplasmic reticulum stress, (5) Srivastava et al. (2014), Stress sensing in plants by an ER stress sensor/transducer, bZIP28, (6) Tintor and Saijo (2014), ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants, (7) Verchot (2014), The ER quality control and ER associated degradation machineries are vital for viral pathogenesis, (8) Nakano et al. (2014), ER bodies in plants of the Brassicales order: biogenesis and association with innate immunity, (9) Höwing et al. (2014), Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense, (10) Williams et al. (2014), When supply does not meet demand-ER stress and plant programmed cell death, (11) Cai et al. (2014), Endoplasmic reticulum stress-induced PCD and caspase-like activities involved.
Mentions: The endoplasmic reticulum (ER) is a very versatile organelle. Besides its major role as the gateway to the secretory pathway the ER is central to adaptation against abiotic and biotic stress. Here, we summarize the current knowledge on ER dynamics and architecture, the association and interaction of the ER with other organelles as well as its role in stress translation and adaptation (Figure 1).

View Article: PubMed Central - PubMed

Affiliation: Plant Research Laboratory, Department of Energy, Michigan State University East Lansing, MI, USA.

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

The ER is a dynamic network of membrane tubules and sheets... Movement of the ER along the actin cytoskeleton has a significant influence on both its architecture and dynamics... To insure that only correctly folded proteins are exported from the ER, eukaryotes have evolved ER quality control (ERQC) mechanisms, which supervise the folding process... Protein folding is monitored through the stepwise modification of oligosaccharide side chains on glycoproteins, and proteins that fail to fold correctly are extracted from the folding process and subjected to ER associated degradation (ERAD)... Srivastava et al. describe the structure of bZIP28 and underlying principles of bZIP28 mobilization in response to stress... ER stress activates the unfolded proteins response (UPR) and the ERAD system to eliminate misfolded proteins, which is vital for the establishment of an effective immune system... The overall significance of the ER in stress adaption is however apparent and underlined by the review of Nakano et al. which, in addition to the biogenesis and evolution, discusses the putative function of ER bodies in abiotic and biotic stress... As ER-derived compartments ER bodies contain stress-associated proteins (e.g., various β-glucosidases of the PYK10 family) that are thought to enhance stress resilience by activating glucosinolates and glucosylated phytohormones... Cells mount adaptive responses (e.g., UPR) to mitigate the damage caused by ER stress... Williams et al. review the possible links between the UPR and PCD and discuss the involvement of calcium signaling and N-rich proteins in promoting PCD and the role of ER chaperones in limiting it as well as the connection of pathogens to ER-mediated cell death... Cai et al. finally compare the activation and/or regulation of ER stress-induced PCD in animals and plants and highlight the significance of caspase and caspase-like activities in underlying PCD processes... By providing a stable microenvironment for the synthesis of metabolites and secreted proteins, the ER functions as an intracellular stress sensory organelle and, accordingly, initiates and regulates adaptive responses to environmental stress... Understanding the molecular basis of these processes and the role of ER architectural dynamics therein is of high relevance for sustainable crop production... We hope our e-book will stimulate research in the field to further enhance our knowledge of ER biology in plants.

No MeSH data available.


Related in: MedlinePlus