ArticleThe Journal of biological chemistry2010
Calcium as a crucial cofactor for low density lipoprotein receptor folding in the endoplasmic reticulum.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes.eLife · 2020Article
- PDI Family Members as Guides for Client Folding and Assembly.International journal of molecular sciences · 2020Review
- Observing the nonvectorial yet cotranslational folding of a multidomain protein, LDL receptor, in the ER of mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Proteostasis Regulation in the Endoplasmic Reticulum: An Emerging Theme in the Molecular Pathology and Therapeutic Management of Familial Hypercholesterolemia.Frontiers in genetics · 2020Review
- Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis.Cold Spring Harbor perspectives in biology · 2019Review
- Identification of amino acid residues in the ligand binding repeats of LDL receptor important for PCSK9 binding.Journal of lipid research · 2019Article
- Cochaperone Mzb1 is a key effector of Blimp1 in plasma cell differentiation and β1-integrin function.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- ER-to-Golgi blockade of nascent desmosomal cadherins in SERCA2-inhibited keratinocytes: Implications for Darier's disease.Traffic (Copenhagen, Denmark) · 2017Article
- Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.The EMBO journal · 2017Article
- Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor.PloS one · 2015Article
- Two phases of disulfide bond formation have differing requirements for oxygen.The Journal of cell biology · 2013Article
- ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor.Molecular cell · 2013Article
- Protein folding in the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Update on the protective molecular pathways improving pancreatic beta-cell dysfunction.Mediators of inflammation · 2013Review
- Protein secretion and the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012Review
- PPAR-γ activation restores pancreatic islet SERCA2 levels and prevents β-cell dysfunction under conditions of hyperglycemic and cytokine stress.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Endoplasmic reticulum stress and the unfolded protein response in nonalcoholic fatty liver disease.Antioxidants & redox signaling · 2011Review
- Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking.Journal of cell science · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family of low density lipoprotein (LDL) receptors mediate uptake of a plethora of ligands from the circulation and couple this to signaling, thereby performing a crucial role in physiological processes including embryonic development, cancer development, homeostasis of lipoproteins, viral infection, and neuronal plasticity. Structural integrity of individual ectodomain modules in these receptors depends on calcium, and we showed before that the LDL receptor folds its modules late after synthesis via intermediates with abundant non-native disulfide bonds and structure. Using a radioactive pulse-chase approach, we here show that for proper LDL receptor folding, calcium had to be present from the very early start of folding, which suggests at least some native, essential coordination of calcium ions at the still largely non-native folding phase. As long as the protein was in the endoplasmic reticulum (ER), its folding was reversible, which changed only upon both proper incorporation of calcium and exit from the ER. Coevolution of protein folding with the high calcium concentration in the ER may be the basis for the need for this cation throughout the folding process even though calcium is only stably integrated in native repeats at a later stage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.