Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Mol Biol Cell 2021 Dec 01;3222:ar37. doi: 10.1091/mbc.E21-03-0146-T.
Show Gene links Show Anatomy links

L-bodies are RNA-protein condensates driving RNA localization in Xenopus oocytes.

Neil CR , Jeschonek SP , Cabral SE , O'Connell LC , Powrie EA , Otis JP , Wood TR , Mowry KL .

Ribonucleoprotein (RNP) granules are membraneless compartments within cells, formed by phase separation, that function as regulatory hubs for diverse biological processes. However, the mechanisms by which RNAs and proteins interact to promote RNP granule structure and function in vivo remain unclear. In Xenopus laevis oocytes, maternal mRNAs are localized as large RNPs to the vegetal hemisphere of the developing oocyte, where local translation is critical for proper embryonic patterning. Here we demonstrate that RNPs containing vegetally localized RNAs represent a new class of cytoplasmic RNP granule, termed localization-bodies (L-bodies). We show that L-bodies contain a dynamic protein-containing phase surrounding a nondynamic RNA-containing phase. Our results support a role for RNA as a critical component within these RNP granules and suggest that cis-elements within localized mRNAs may drive subcellular RNA localization through control over phase behavior.

PubMed ID: 34613784
Article link: Mol Biol Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: cpeb1 dnai1 gapdh gdf1 hnrnpab igf2bp3 isyna1 kif3a lrwd1 lsm14b lsm2 mtor nos1 padi2 pmch stau1 trim36 vegt ybx1
GO keywords: P-body [+]
Antibodies: Tuba4b Ab2

Article Images: [+] show captions
References [+] :
Ahsan, Highly reproducible improved label-free quantitative analysis of cellular phosphoproteome by optimization of LC-MS/MS gradient and analytical column construction. 2017, Pubmed