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XB-ART-9093
EMBO J 2001 May 01;209:2315-25. doi: 10.1093/emboj/20.9.2315.
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A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization.

Zhao WM , Jiang C , Kroll TT , Huber PW .


Abstract
A 340 nucleotide element within the 3' untranslated region of Vg1 mRNA determines its localization to the vegetal cortex of Xenopus oocytes. To identify protein factors that bind to this region, we screened a cDNA expression library with an RNA probe containing this sequence. Five independent isolates encoded a protein (designated Prrp for proline-rich RNA binding protein) having two RNP domains followed by multiple polyproline segments. Prrp and Vg1 mRNAs are co-localized to the vegetal cortex of stage IV oocytes, substantiating an interaction between the two in vivo. Prrp also associates with VegT mRNA, which like Vg1 mRNA uses the late localization pathway, but not with Xcat-2 or Xwnt-11 mRNAs, which use the early pathway. The proline-rich domain of Prrp interacts with profilin, a protein that promotes actin polymerization. Prrp can also associate with the EVH1 domain of Mena, another microfilament-associated protein. Since the anchoring of Vg1 mRNA to the vegetal cortex is actin dependent, one function of Prrp may be to facilitate local actin polymerization, representing a novel function for an RNA binding protein.

PubMed ID: 11331596
PMC ID: PMC125447
Article link: EMBO J


Species referenced: Xenopus
Genes referenced: actl6a gdf1 pfn1 prlh vegt

References [+] :
Ahern-Djamali, Identification of profilin and src homology 3 domains as binding partners for Drosophila enabled. 1999, Pubmed