Prion protein interaction with stress-inducible protein 1 enhances neuronal protein synthesis via mTOR

Roffé, Martín; Beraldo, Flávio H.; Bester, Romina; Nunziante, Max; Bach, Christian; Mancini, Gabriel L.; Gilch, Sabine; Vorberg, Ina; Castilho, Beatriz A.; Martins, Vilma R.; Hajj, Glaucia Noeli Maroso

doi:10.1073/pnas.1000784107

Cited by 97 publications

(89 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies done using cell lines and primary neuronal cells infected with homogenate from prion infected mice showed a significant increase in eIF2α phosphorylation [33]. The same was observed by Moreno, et al when using PrP TSE infected mice [26].…”

Section: The Role Of Perk and Eif2αsupporting

confidence: 69%

“…Steady state protein levels of PrP are directly dependent on ERp57 expression using gain-of and loss-of-function in vivo and in vitro experiments [51]. Interestingly, loss of ERp57 results in the activation of the UPR via PERK [52], and the PERK/ eIF2α pathway promotes prion disease [25,26,33]. There is potential for ERp57 being a therapeutic target to treat prion diseases and other protein misfolding disorders since ERp57 has been implicated in other neurological diseases such as Alzheimer's disease (AD), Parkinson's disease (PD) , and amyotrophic lateral sclerosis (ALS) [53].…”

Section: Additional Er Stress Molecules and Prion Diseasementioning

confidence: 99%

See 1 more Smart Citation

Prion disease and endoplasmic reticulum stress pathway correlations and treatment pursuits

Satterfield

Pritchett

Cruz

et al. 2017

Endoplasmic Reticulum Stress in Diseases

View full text Add to dashboard Cite

Background: Transmissible spongiform encephalopathies are a collection of rare neurodegenerative disorders characterized by loss of neuronal cells, astrocytosis, and plaque formation. The causative agent of these diseases is thought to be abnormally folded prions and is characterized by a conformational change from normal, cellular prion protein (PrPc) to the abnormal form (PrPTSE). Although, there is evidence that normal prion protein can contribute to these disorders. The unfolded protein response, a conserved series of pathways involved in resolving stress associated with unfolded protein accumulation in the Endoplasmic Reticulum (ER), has been shown to play a role in regulating the development of prion diseases. Methods: This review chose papers based on their relevance to current studies involved in prion protein synthesis and transformation, identifies various links between prion diseases and ER stress, and reports on current and potential treatments as they relate to ER stress and prion diseases. Conclusion: For the advancement of prion disease treatment, it is important to understand the mechanisms involved in prion formation, and ER stress is implicated in prion disease progression. Therefore, targeting the ER or pathways involved in response to stress in the ER may help us treat prion diseases.

show abstract

Section: The Role Of Perk and Eif2αsupporting

confidence: 69%

Section: Additional Er Stress Molecules and Prion Diseasementioning

confidence: 99%

Prion disease and endoplasmic reticulum stress pathway correlations and treatment pursuits

Satterfield

Pritchett

Cruz

et al. 2017

Endoplasmic Reticulum Stress in Diseases

View full text Add to dashboard Cite

show abstract

“…PrP C was also pointed to protect neurons against injury both in vitro and in vivo (13,19,25). PrP C protein is itself a receptor for the secreted form of STI1, an interaction that has been shown to promote neuroprotection and neuronal differentiation (25,68,69). Our present data indicate that Ln ␥1 peptide impaired staurosporine-induced cell death in PrP3F4 cells, whereas Ln ␥1 peptide fails to rescue CF10 and CF10 cells expressing PrP C mutants from death.…”

Section: Discussionmentioning

confidence: 42%

Disease-associated Mutations in the Prion Protein Impair Laminin-induced Process Outgrowth and Survival

Machado

Beraldo

Santos

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: In addition to the toxicity mediated by prion protein misfolding, mechanisms associated with its loss-offunction in genetic prion diseases are unknown. Results: Neural cells expressing PrP C mutants associated with prion diseases present impaired laminin-mediated process outgrowth and survival. Conclusion: PrP C mutants show loss-of-function in neural cells. Significance: The impairment of prion protein functions may contribute to the etiology of prion diseases.

show abstract

“…[5][6][7] Some PRNP interactions take place in lipid raft microdomains such as those involving NCAM (neural cell adhesion molecule) and CAV1/caveolin-1, which couple PRNP to the tyrosine kinase FYN (Fyn proto-oncogene). 8,9 These complexes modulate neuroprotection against cellular and systemic insults, [10][11][12] participate in cell signaling cascades, 13 promote neuritogenesis, 14 regulate neuronal plasticity, excitability, memory formation, and consolidation, 15 and mediate synaptic vesicle transmission. 16 PRNP is abundantly expressed in neuronal cells, but has also been observed in non-neuronal cells.…”

Section: Introductionmentioning

confidence: 99%

PRNP/prion protein regulates the secretion of exosomes modulating CAV1/caveolin-1-suppressed autophagy

et al. 2016

Self Cite

View full text Add to dashboard Cite

Prion protein modulates many cellular functions including the secretion of trophic factors by astrocytes. Some of these factors are found in exosomes, which are formed within multivesicular bodies (MVBs) and secreted into the extracellular space to modulate cell-cell communication. The mechanisms underlying exosome biogenesis were not completely deciphered. Here, we demonstrate that primary cultures of astrocytes and fibroblasts from prnp-null mice secreted lower levels of exosomes than wild-type cells. Furthermore, prnp-null astrocytes exhibited reduced MVB formation and increased autophagosome formation. The reconstitution of PRNP expression at the cell membrane restored exosome secretion in PRNP-deficient astrocytes, whereas macroautophagy/autophagy inhibition via BECN1 depletion reestablished exosome release in these cells. Moreover, the PRNP octapeptide repeat domain was necessary to promote exosome secretion and to impair the formation of the CAV1-dependent ATG12-ATG5 cytoplasmic complex that drives autophagosome formation. Accordingly, higher levels of CAV1 were found in lipid raft domains instead of in the cytoplasm in prnp-null cells. Collectively, these findings demonstrate that PRNP supports CAV1-suppressed autophagy to protect MVBs from sequestration into phagophores, thus facilitating exosome secretion.

show abstract

Prion protein interaction with stress-inducible protein 1 enhances neuronal protein synthesis via mTOR

Cited by 97 publications

References 43 publications

Prion disease and endoplasmic reticulum stress pathway correlations and treatment pursuits

Prion disease and endoplasmic reticulum stress pathway correlations and treatment pursuits

Disease-associated Mutations in the Prion Protein Impair Laminin-induced Process Outgrowth and Survival

PRNP/prion protein regulates the secretion of exosomes modulating CAV1/caveolin-1-suppressed autophagy

Contact Info

Product

Resources

About