Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

Brostrom, Margaret A.; Brostrom, Charles O.

doi:10.1016/s0143-4160(03)00127-1

Cited by 188 publications

(140 citation statements)

References 116 publications

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“…These data agree well with the predictions made by the model. ER stress response is a hallmark of global depletion of ER Ca 2ϩ and has been reported to occur in cells treated with relatively high concentrations of Tg and agonists, within the range used to activate SOCE (33,34). One of the earliest events in the unfolded protein response to ER stress is activation of the kinase PERK, which leads to inhibition of protein synthesis.…”

Section: Depletion Of Peripheral Ca 2ϩmentioning

confidence: 99%

Relocalization of STIM1 for Activation of Store-operated Ca2+ Entry Is Determined by the Depletion of Subplasma Membrane Endoplasmic Reticulum Ca2+ Store

Ong

Liu

Tsaneva-Atanasova

et al. 2007

Journal of Biological Chemistry

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entering the cell is rapidly taken up into the ER by SERCA activity with minimal diffusion in the subplasma membrane region. These studies indicate close apposition of the ER and plasma membrane at the site of SOCE (1-6). Thus, it has been suggested that ER localized in the subplasma membrane region is likely to be coupled to SOCE and that depletion of these local Ca 2ϩ stores triggers activation of SOCE. The presently proposed mechanisms for activation of SOCE suggest direct physical coupling between components in the ER and plasma membrane, generation of diffusible components, or recruitment of the SOC channel. The exact mechanism involved in regulation of SOCE as well as the molecular components of the channel(s) mediating Ca 2ϩ entry in different types of cells has not been clearly identified.Recent studies have suggested STIM1 (stromal interacting molecule 1) as a novel regulator for SOCE. STIM1, which is a Ca 2ϩ -binding protein localized diffusely in the ER, has been shown to relocate into a peripheral region of the cell in response to internal Ca 2ϩ store depletion (7,8). STIM1 displays punctate subplasma membrane localization in response to depletion of intracellular Ca 2ϩ stores, which has been reported to be causal in activation of SOCE and to define the elementary unit that is involved in SOCE. Although several studies have clearly established involvement of ER-plasma membrane junctional domains in the regulation of SOCE, the exact site of store depletion has not yet been demonstrated. Based on all of the data available presently, it is logical to propose that that since the EF-hand domain of STIM1 is localized in the lumen of the ER and STIM1 punctae involved in SOCE activation are localized in subplasma membrane Ca 2ϩ stores very close to the surface * The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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Section: Depletion Of Peripheral Ca 2ϩmentioning

confidence: 99%

Relocalization of STIM1 for Activation of Store-operated Ca2+ Entry Is Determined by the Depletion of Subplasma Membrane Endoplasmic Reticulum Ca2+ Store

Ong

Liu

Tsaneva-Atanasova

et al. 2007

Journal of Biological Chemistry

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“…Ca 2ϩ release via ryanodine or inositol 1,4,5-trisphosphate (IP 3 ) receptors regulates excitability, neuronal differentiation, and some forms of synaptic plasticity (for review, see Berridge, 1998;Verkhratsky, 2005). Furthermore, Ca 2ϩ sequestered within the ER is essential for maintaining protein synthesis (Brostrom and Brostrom, 2003), whereas chronic Ca 2ϩ overload of the stores is implicated in some neurological disorders (Paschen, 2003;Verkhratsky, 2005). Thus, SERCA-mediated Ca 2ϩ sequestration is a critical component of neuronal signaling.…”

Section: Introductionmentioning

confidence: 99%

Activation of Protein Kinase C in Sensory Neurons Accelerates Ca²⁺Uptake into the Endoplasmic Reticulum

Usachev

Marsh

Johanns³

et al. 2006

J. Neurosci.

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“…Release of Ca 2ϩ into the cytosol mediated by SERCA inhibitors such as thapsigargin and curcumin rescues the transport of some misfolded proteins, most likely by affecting chaperone functions (34,35). We have shown here that the CPPs penetratin and KLAL, but not the TAT peptide, also increase cytosolic Ca 2ϩ concentrations, indicating that the peptide-mediated rescue is associated with these changes.…”

Section: Discussionmentioning

confidence: 58%

Rescue of a Nephrogenic Diabetes Insipidus-causing Vasopressin V2 Receptor Mutant by Cell-penetrating Peptides

Oueslati

Hermosilla

Schönenberger

et al. 2007

Journal of Biological Chemistry

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Mutant membrane proteins are frequently retained in the early secretory pathway by a quality control system, thereby causing disease. An example are mutants of the vasopressin V 2 receptor (V 2 R) leading to nephrogenic diabetes insipidus. Transport-defective V 2 Rs fall into two classes: those retained exclusively in the endoplasmic reticulum (ER) and those reaching post-ER compartments such as the ER/Golgi intermediate compartment. Although numerous chemical or pharmacological chaperones that rescue the transport of ER-retained membrane proteins are known, substances acting specifically in post-ER compartments have not been described as yet. Using the L62P (ER-retained) and Y205C (reaching post-ER compartments) mutants of the V 2 R as a model, we show here that the cell-penetrating peptide penetratin and its synthetic analog KLAL rescue the transport of the Y205C mutant. In contrast, the location of the L62P mutant is not influenced by either peptide because the peptides are unable to enter the ER. We also show data indicating that the peptide-mediated transport rescue is associated with an increase in cytosolic Ca 2؉ concentrations. Thus, we describe a new class of substances influencing protein transport specifically in post-ER compartments.The hormone 8-arginine vasopressin (AVP 2 ; antidiuretic hormone) mediates water reabsorption in the kidney via the G protein-coupled human vasopressin V 2 receptor (V 2 R) located at the cell surface (1, 2). Mutations in the V 2 R gene cause X-linked nephrogenic diabetes insipidus (NDI), a disease characterized by the kidney's inability to concentrate urine. The majority of the mutations result in transport-defective receptors (3), which are recognized and intracellularly retained by the quality control system (QCS). Besides NDI, transportdefective membrane proteins play a role in many other diseases (4, 5).The QCS is located mainly in the endoplasmic reticulum (ER) and allows only correctly folded and/or assembled proteins to leave the early secretory pathway and to reach their final cellular destination (6, 7). Several components have been described to contribute to the QCS: (i) the lectin chaperones calnexin and calreticulin involved in the quality control of glycoproteins; (ii) "classical" chaperones such as the IgG heavy chain-binding protein, endoplasmin/grp90, and the ER-resident DnaJ-like proteins ERdj1-ERdj5; and (iii) enzymes such as protein-disulfide isomerase and the thiol oxidoreductase ERp57 (8). Misfolded or unassembled membrane proteins initially display a prolonged association with components of the QCS. They may then either accumulate in the ER, leading to the unfolded protein response (9), and/or be subjected to proteasomal degradation (10,11). It has also been demonstrated that the QCS is not restricted to the ER but involves post-ER compartments such as the ER/Golgi intermediate compartment (ERGIC) (12, 13). For the V 2 R, we have shown recently that transport-defective mutant receptors fall into two classes: mutants like L62P are retained exclusivel...

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Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

Cited by 188 publications

References 116 publications

Relocalization of STIM1 for Activation of Store-operated Ca2+ Entry Is Determined by the Depletion of Subplasma Membrane Endoplasmic Reticulum Ca2+ Store

Relocalization of STIM1 for Activation of Store-operated Ca2+ Entry Is Determined by the Depletion of Subplasma Membrane Endoplasmic Reticulum Ca2+ Store

Activation of Protein Kinase C in Sensory Neurons Accelerates Ca²⁺Uptake into the Endoplasmic Reticulum

Rescue of a Nephrogenic Diabetes Insipidus-causing Vasopressin V2 Receptor Mutant by Cell-penetrating Peptides

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Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

Cited by 188 publications

References 116 publications

Relocalization of STIM1 for Activation of Store-operated Ca2+ Entry Is Determined by the Depletion of Subplasma Membrane Endoplasmic Reticulum Ca2+ Store

Relocalization of STIM1 for Activation of Store-operated Ca2+ Entry Is Determined by the Depletion of Subplasma Membrane Endoplasmic Reticulum Ca2+ Store

Activation of Protein Kinase C in Sensory Neurons Accelerates Ca2+Uptake into the Endoplasmic Reticulum

Rescue of a Nephrogenic Diabetes Insipidus-causing Vasopressin V2 Receptor Mutant by Cell-penetrating Peptides

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Activation of Protein Kinase C in Sensory Neurons Accelerates Ca²⁺Uptake into the Endoplasmic Reticulum