Proteins aggregates and tumorigenesis

What is it about?

Misfolded proteins are a common outcome of protein biosynthesis in our body cell, and about 30% of newly synthesized proteins end up misfolded. Normally, these misfolded proteins are ubiquitinated and degraded by the proteasome system and/or autophagy process. Multiple factors ranging from genetic mutations (in neurodegeneration) to cellular (oxidative/proteotoxic stress) and environmental stresses can trigger protein misfolding overwhelming the cellular capacity to clear them leading to their aggregation and accumulation resulting in many pathological conditions collectively termed as proteinopathies (Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis, etc.). On the flip side, recent study showed that the augmented capacity to degrade the misfolded proteins alleviates oxidative stress associated with cancerous growth and is required for both the initiation and maintenance of malignant phenotypes (Chen et al. 2017, Cell reports). So the cancer cells hijack the machinery of protein quality control and utilizes them for their survival.

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