Endoplasmic reticulum: The unfolded protein response is tangled in neurodegeneration

The endoplasmic reticulum (ER) is involved in the folding and maturation of membrane-bound and secreted proteins. Disturbed homeostasis in the ER can lead to accumulation of misfolded proteins, which trigger a stress response called the unfolded protein response (UPR). In neurodegenerative diseases...

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Bibliographic Details
Published in:The international journal of biochemistry & cell biology 2012-08, Vol.44 (8), p.1295-1298
Main Authors: Hoozemans, Jeroen J.M., Scheper, Wiep
Format: Article
Language:English
Subjects:
Animals
Apoptosis
Autophagy
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
homeostasis
Humans
microtubules
Models, Biological
Neurodegeneration
neurodegenerative diseases
Neurodegenerative Diseases - metabolism
Neurodegenerative Diseases - pathology
phosphorylation
proteins
Signal Transduction
stress response
tau Proteins - metabolism
Tauopathy
Unfolded Protein Response
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Summary:The endoplasmic reticulum (ER) is involved in the folding and maturation of membrane-bound and secreted proteins. Disturbed homeostasis in the ER can lead to accumulation of misfolded proteins, which trigger a stress response called the unfolded protein response (UPR). In neurodegenerative diseases that are classified as tauopathies, activation of the UPR coincides with the pathogenic accumulation of the microtubule associated protein tau. Several lines of evidence indicate that UPR activation contributes to increased levels of phosphorylated tau, a prerequisite for the formation of tau aggregates. Increased understanding of the crosstalk between signaling pathways involved in protein quality control in the ER and tau phosphorylation will support the development of new therapeutic targets that promote neuronal survival.
ISSN:1357-2725
1878-5875
DOI:10.1016/j.biocel.2012.04.023