The enigmatic ATP supply of the endoplasmic reticulum

Depaoli, Maria R.; Hay, Jesse; Graier, Wolfgang F.; Malli, Roland

doi:10.1111/brv.12469

Cited by 46 publications

(40 citation statements)

References 224 publications

(268 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…While acidocalcisomes store high concentrations of phosphate and are, hence, prime candidates for a P i -buffering system, it must be kept in mind that other organelles also use and/or liberate P i as part of their metabolic functions. For example, the endoplasmic reticulum (ER) lumen contains many chaperones that hydrolyze ATP ( Depaoli et al, 2019 ). The Golgi liberates P i as a by-product of the glycosylation reactions in this compartment, and it is likely that this P i is recycled back to the cytosol through a dedicated channel, Erd1 ( Snyder et al, 2017 ).…”

Section: Acidocalcisomes: a Conserved Organelle With A Role In Phosphmentioning

confidence: 99%

Phosphate Homeostasis − A Vital Metabolic Equilibrium Maintained Through the INPHORS Signaling Pathway

Austin

Mayer

2020

Front. Microbiol.

View full text Add to dashboard Cite

Cells face major changes in demand for and supply of inorganic phosphate (P i ). P i is often a limiting nutrient in the environment, particularly for plants and microorganisms. At the same time, the need for phosphate varies, establishing conflicts of goals. Cells experience strong peaks of P i demand, e.g., during the S-phase, when DNA, a highly abundant and phosphate-rich compound, is duplicated. While cells must satisfy these P i demands, they must safeguard themselves against an excess of P i in the cytosol. This is necessary because P i is a product of all nucleotide-hydrolyzing reactions. An accumulation of P i shifts the equilibria of these reactions and reduces the free energy that they can provide to drive endergonic metabolic reactions. Thus, while P i starvation may simply retard growth and division, an elevated cytosolic P i concentration is potentially dangerous for cells because it might stall metabolism. Accordingly, the consequences of perturbed cellular P i homeostasis are severe. In eukaryotes, they range from lethality in microorganisms such as yeast ( Sethuraman et al., 2001 ; Hürlimann, 2009 ), severe growth retardation and dwarfism in plants ( Puga et al., 2014 ; Liu et al., 2015 ; Wild et al., 2016 ) to neurodegeneration or renal Fanconi syndrome in humans ( Legati et al., 2015 ; Ansermet et al., 2017 ). Intracellular P i homeostasis is thus not only a fundamental topic of cell biology but also of growing interest for medicine and agriculture.

show abstract

Section: Acidocalcisomes: a Conserved Organelle With A Role In Phosphmentioning

confidence: 99%

Phosphate Homeostasis − A Vital Metabolic Equilibrium Maintained Through the INPHORS Signaling Pathway

Austin

Mayer

2020

Front. Microbiol.

View full text Add to dashboard Cite

show abstract

“…The first arm of the protein quality control system, protein synthesis, controls translation of mRNA into protein. Ribosomes, located both in the rough ER and freely in the cytosol, shepherd the transition of mRNA to protein (Ainsley et al, 2014;Depaoli et al, 2018). Often organized in complexes comprised of many individual ribosomal subunits (Genuth and Barna, 2018), ribosomes interact with a variety of other proteins, including Ribosomal Associated Proteins (RAPs), kinases, and phosphatases, which facilitate the production of all proteins in the cell (Heise et al, 2014;Genuth and Barna, 2018).…”

Section: Protein Synthesismentioning

confidence: 99%

Homeostatic Roles of the Proteostasis Network in Dendrites

Lottes

Cox

2020

Front. Cell. Neurosci.

View full text Add to dashboard Cite

Cellular protein homeostasis, or proteostasis, is indispensable to the survival and function of all cells. Distinct from other cell types, neurons are long-lived, exhibiting architecturally complex and diverse multipolar projection morphologies that can span great distances. These properties present unique demands on proteostatic machinery to dynamically regulate the neuronal proteome in both space and time. Proteostasis is regulated by a distributed network of cellular processes, the proteostasis network (PN), which ensures precise control of protein synthesis, native conformational folding and maintenance, and protein turnover and degradation, collectively safeguarding proteome integrity both under homeostatic conditions and in the contexts of cellular stress, aging, and disease. Dendrites are equipped with distributed cellular machinery for protein synthesis and turnover, including dendritically trafficked ribosomes, chaperones, and autophagosomes. The PN can be subdivided into an adaptive network of three major functional pathways that synergistically govern protein quality control through the action of (1) protein synthesis machinery; (2) maintenance mechanisms including molecular chaperones involved in protein folding; and (3) degradative pathways (e.g., Ubiquitin-Proteasome System (UPS), endolysosomal pathway, and autophagy. Perturbations in any of the three arms of proteostasis can have dramatic effects on neurons, especially on their dendrites, which require tightly controlled homeostasis for proper development and maintenance. Moreover, the critical importance of the PN as a cell surveillance system against protein dyshomeostasis has been highlighted by extensive work demonstrating that the aggregation and/or failure to clear aggregated proteins figures centrally in many neurological disorders. While these studies demonstrate the relevance of derangements in proteostasis to human neurological disease, here we mainly review recent literature on homeostatic developmental roles the PN machinery plays in the establishment, maintenance, and plasticity of stable and dynamic dendritic arbors. Beyond basic housekeeping functions, we consider roles of PN machinery in protein quality control mechanisms linked to dendritic plasticity (e.g., dendritic spine remodeling during LTP); cell-type specificity; dendritic morphogenesis; and dendritic pruning.

show abstract

“…Retention of thyroglobulin, or in general of any protein, will lead to a response via the endoplasmic reticulum in the sense of the unfolded protein response [82,83] . This process requires sufficient ATP supply [84] . In 3 of their publications, Barishev et al [85,86] Sargsyan et al [87] described the mechanisms involved in congenital hypothyroidism.…”

Section: An Interlude: Updating the Contribution Of Geneticsmentioning

confidence: 99%