A compact regulatory RNA element in mouse Hsp70 mRNA.

Hsp70 (70 kDa heat shock protein) performs molecular chaperone functions by assisting the folding of newly synthesized and misfolded proteins, thereby counteracting various cell stresses and preventing multiple diseases, including neurodegenerative disorders and cancers. It is well established that, immediately after heat shock, Hsp70 gene expression is mediated by a canonical mechanism of cap-dependent translation. However, the molecular mechanism of Hsp70 expression during heat shock remains elusive.

Localized molecular chaperone synthesis maintains neuronal dendrite proteostasis.

Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. Using high-resolution fluorescence microscopy, we discovered that neurons localize a subset of chaperone mRNAs to their dendrites and use microtubule-based transport to increase this asymmetric localization following proteotoxic stress.

A compact regulatory RNA element in mouse Hsp70 mRNA.

Hsp70 performs molecular chaperone functions by assisting in folding newly synthesized or misfolded proteins, thereby counteracting various cell stresses and preventing multiple diseases including neurodegenerative disorders and cancer. It is well established that Hsp70 upregulation during post-heat shock stimulus is mediated by cap-dependent translation. However, the molecular mechanisms of Hsp70 expression during heat shock stimulus remains elusive, even though the 5' end of Hsp70 mRNA may form a compact structure to positively regulate protein expression in the mode of cap-independent translation.