Abstract:Graphical Abstract Highlights d Cytoplasmic YBX1_IMP1 mRNP granules are elongated and branched structures d mRNPs are formed at the nuclear pore and await translation d Small cytoplasmic IMP1 and YBX1 mRNPs are mRNA singletons SUMMARY Small cytoplasmic mRNP granules are implicated in mRNA transport, translational control, and decay. Using super-resolution microscopy and fluorescence correlation spectroscopy, we analyzed the molecular composition and dynamics of single cytoplasmic YBX1_IMP1 mRNP granules in liv… Show more
“…However, the exact role of YB-1 in this process is unknown. Recently, it was found that even though YB-1 and IGF2BP1 do not interact directly, they bind the same mRNA molecules immediately after mRNA nuclear export [142].…”
Section: Yb Proteins In Mrna Stability Controlmentioning
Y-box binding proteins (YB proteins) are DNA/RNA-binding proteins belonging to a large family of proteins with the cold shock domain. Functionally, these proteins are known to be the most diverse, although the literature hardly offers any molecular mechanisms governing their activities in the cell, tissue, or the whole organism. This review describes the involvement of YB proteins in RNA-dependent processes, such as mRNA packaging into mRNPs, mRNA translation, and mRNA stabilization. In addition, recent data on the structural peculiarities of YB proteins underlying their interactions with nucleic acids are discussed.
“…However, the exact role of YB-1 in this process is unknown. Recently, it was found that even though YB-1 and IGF2BP1 do not interact directly, they bind the same mRNA molecules immediately after mRNA nuclear export [142].…”
Section: Yb Proteins In Mrna Stability Controlmentioning
Y-box binding proteins (YB proteins) are DNA/RNA-binding proteins belonging to a large family of proteins with the cold shock domain. Functionally, these proteins are known to be the most diverse, although the literature hardly offers any molecular mechanisms governing their activities in the cell, tissue, or the whole organism. This review describes the involvement of YB proteins in RNA-dependent processes, such as mRNA packaging into mRNPs, mRNA translation, and mRNA stabilization. In addition, recent data on the structural peculiarities of YB proteins underlying their interactions with nucleic acids are discussed.
“…2 and 34 molecules with a median of 5-8 (Mateu-Regué et al 2019). Each RNA-binding protein may recruit several effector proteins, thus generating a niche.…”
Section: Lu Lu-f1 Lu-f2 Lu-f3mentioning
confidence: 99%
“…It has long been thought that "mRNA regulons" exist, in which functionally related groups of mRNAs are coregulated (Keene 2007). However, there is recent evidence that cytoplasmic mRNP (messenger RNA nucleoprotein complex) granules consist of single mRNAs, which would preclude coregulation of mRNAs (Mateu-Regué et al 2019). However, formation of larger mRNA granules such as TIS granules that contain many mRNAs may enable the mingling of different mRNAs to allow coregulation as well as coor peritranslational protein complex assembly of transcripts that are translated in vicinity to each other (…”
Messenger RNAs (mRNAs) are the templates for protein synthesis as the coding region is translated into the amino acid sequence. mRNAs also contain 3 0 untranslated regions (3 0 UTRs) that harbor additional elements for the regulation of protein function. If the amino acid sequence of a protein is necessary and sufficient for its function, we call it 3 0 UTR-independent. In contrast, functions that are accomplished by protein complexes whose formation requires the presence of a specific 3 0 UTR are 3 0 UTR-dependent protein functions. We showed that 3 0 UTRs can regulate protein activity without affecting protein abundance, and alternative 3 0 UTRs can diversify protein functions. We currently think that the regulation of protein function by 3 0 UTRs is facilitated by the local environment at the site of protein synthesis, which we call the nurturing niche for nascent proteins. This niche is composed of the mRNA and the bound proteins that consist of RNA-binding proteins and recruited proteins. It enables the formation of specific protein complexes, as was shown for TIS granules, a recently discovered cytoplasmic membraneless organelle. This finding suggests that changing the niche for nascent proteins will alter protein activity and function, implying that cytoplasmic membraneless organelles can regulate protein function in a manner that is independent of protein abundance.
“…Super‐resolution microscopy has recently given a more detailed outline of pre‐translational mRNPs. In contrast to the spherical appearance (“granular”) derived from conventional confocal microscopy, Structured Illumination Microscopy has shown that pre‐translational mRNPs are branched and elongated structures, [ 12 ] ranging from 100 to 1000 nm in size. [ 13,14 ] The mRNPs are composed of a single mRNA and one or two handfuls of RBPs which is in fine agreement with their size.…”
Section: Architecture and Dimensions Of Cytoplasmic Mrnpsmentioning
Cytoplasmic messenger ribonucleoprotein particles (mRNPs) represent the cellular transcriptome, and recent data have challenged our current understanding of their architecture, transport, and complexity before translation. Pre-translational mRNPs are composed of a single transcript, whereas P-bodies and stress granules are condensates. Both pre-translational mRNPs and actively translating mRNPs seem to adopt a linear rather than a closed-loop configuration. Moreover, assembly of pre-translational mRNPs in physical RNA regulons is an unlikely event, and co-regulated translation may occur locally following extracellular cues. We envisage a stochastic mRNP transport mechanism where translational repression of single mRNPs-in combination with microtubule-mediated cytoplasmic streaming and docking events-are prerequisites for local translation, rather than direct transport.
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