There are two sets of protein translation systems in mammalian cells —
the cytoplasmic translation system and the mitochondrial translation system — both of which are composed of ribosome, tRNAs and translation factors.
In order to keep step with the «quickened» mitochondrial translation, somatic cells activated the mTOR signaling pathway in order to accelerate
cytoplasmic translation and balance mitochondrial translation.
It describes the crosstalk mechanism between mitochondrial translation and
cytoplasmic translation.
«Study unveils novel crosstalk mechanism between mitochondrial translation and
cytoplasmic translation.»
However, the coordination mechanism between
the cytoplasmic translation system and the mitochondrial translation system has been a mystery.
Not exact matches
When the mitochondrial
translation rate increases, the mTOR signaling pathway is activated, which causes the increase in the
cytoplasmic protein
translation rate to counteract pressure from the increased mitochondrial
translation, thus representing a new evolutionary adaptation mechanism.
Headed by ICREA Research Professor Raúl Méndez, an expert on the CPEB (
cytoplasmic polyadenylation element binding protein) protein family, this study reveals the interplay between the proteins CPEB1 and Musashi1 (Msi1) in the regulation of mRNA
translation.
Here we report that the
cytoplasmic polyadenylation element binding protein 1 (CPEB1), an RNA - binding protein that regulates mRNA
translation, also controls alternative 3 ′ - UTR processing.
CPEB (
Cytoplasmic Polyadenylation Element Binding) proteins are a family of four RNA - binding proteins that regulate the
translation of maternal mRNAs controlling meiotic cell cycle progression.
«Cells respond to different types of stress by inhibition of protein synthesis and subsequent assembly of stress granules (SGs),
cytoplasmic aggregates that contain stalled
translation preinitiation complexes.