In: Cell Stress and Chaperones, 2015, vol. 20, no. 4, p. 605-620
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In: FEBS Letters, 2020, vol. 594, no. 23, p. 3986-4000
Post-transcriptional regulation of ATP-binding cassette (ABC) proteins has been so far shown to encompass protein phosphorylation, maturation, and ubiquitination. Yet, recent accumulating evidence implicates FK506-binding proteins (FKBPs), a type of peptidylprolyl cis–trans isomerase (PPIase) proteins, in ABC transporter regulation. In this perspective article, we summarize current knowledge on...
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In: FEBS Letters, 2019, vol. 593, no. 13, p. 1415–1430
In order to survive under ever‐changing conditions plants must be able to adaptively respond to their environment. Plant hormones and the signaling cross‐talk among them play a key role in integrating external and internal cues, enabling the plants to acclimate accordingly. HSP90 and several of its co‐chaperones are known as pleiotropic factors involved in the signaling pathways of...
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In: AIMS biophysics, 2016, vol. 3, no. 4, p. 456-478
The biosynthesis of proteins entails a complex series of chemical reactions that transform the information stored in the nucleic acid sequence into a polypeptide chain that needs to properly fold and reach its functional location in or outside the cell. It is of no surprise that errors might occur that alter the polypeptide sequence leading to a non-functional proteins or that impede delivery...
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In: Swiss medical weekly, 2014, vol. 144, p. w14001
The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells proteome. The capacity to produce correctly folded polypeptides and to transport them to their correct intra- or extracellular destinations relies on proteostasis networks that regulate and balance the...
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In: European Spine Journal, 2014, vol. 23, no. 9, p. 1878-1891
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In: International Journal of Colorectal Disease, 2014, vol. 29, no. 6, p. 663-671
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In: Cellular and Molecular Life Sciences, 2014, vol. 71, no. 17, p. 3311-3325
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In: Cell Stress and Chaperones, 2014, vol. 19, no. 1, p. 83-90
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In: Journal of biological chemistry, 2018, vol. 293, no. 15, p. 5600-5612
The stress sensors ATF6, IRE1, and PERK monitor deviations from homeostatic conditions in the endoplasmic reticulum (ER), a protein biogenesis compartment of eukaryotic cells. Their activation elicits unfolded protein responses (UPR) to reestablish proteostasis. UPR have been extensively investigated in cells exposed to chemicals that activate ER stress sensors by perturbing calcium, N-glycans,...
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