Importantly, the identified yeast mRNP proteins and proteome of SGs cores are highly conserved between yeast and mammals [9, 33].
The persistent mRNP granules could impair ribostasis and cause other pathological changes in the cells.
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(1) ATP-driven disaggregases: the yeast Hsp104 disaggregase is an essential protein that dissolves SGs and thereby maintains the integrity of other mRNPs such as PBs by preventing their entry into SGs [27, 28].
(4) PBs: PBs affect the assembly of SGs because PBs and SGs are spatially linked and constantly exchange mRNPs [4,10,13,39].
Our aim is to gather structural information of mRNP complexes involved in RNA localization in the fruit fly Drosophila, currently the best-studied model system.
The correct cytoplasmic localization of mRNAs and their transport and silencing in messenger ribonucleoprotein particles (mRNPs), is dependent on the earliest steps of mRNA processing in the nucleus.