Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3′-untranslated region by the mRNA endonuclease polysomal ribonuclease 1

Cunningham, Kristopher S.; Dodson, Robin E.; Nagel, Maria A.; Shapiro, David J.; Schoenberg, Daniel R.

doi:10.1073/pnas.220425497

Cited by 77 publications

(77 citation statements)

References 27 publications

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“…Northwestern blot analyses with Scp160p demonstrated RNA binding activity in vitro with low sequence specificity (24). RNA gel mobility shift assays and mRNA affinity column chromatography showed that Xenopus vigilin binds specifically to the 3Ј-untranslated region of vitellogenin mRNA (23,25), stabilizing the RNA by blocking cleavage by an endonuclease (26). In contrast to these results, Kruse et al (27,28) propose that human vigilin may be involved in binding and transport of tRNA.…”

mentioning

confidence: 99%

Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner

Frey

Pool

Seedorf

2001

Journal of Biological Chemistry

102

116

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Scp160p is an RNA-binding protein containing 14 tandemly repeated heterogenous nuclear ribonucleoprotein K-homology domains, which are implicated in RNA binding. Scp160p interacts with free and membranebound polysomes that are dependent upon the presence of mRNA. Despite its presence on cytosolic polysomes, Scp160p is predominantly localized to the endoplasmic reticulum (ER). Accumulation of Scp160p-ribosome complexes at the ER requires the function of microtubules but is independent of the actin cytoskeleton. We propose that the multi-K-homology-domain protein Scp160p functions as an RNA binding platform, interacting with polysomes that are transported to the ER.

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mentioning

confidence: 99%

Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner

Frey

Pool

Seedorf

2001

Journal of Biological Chemistry

102

116

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“…Examples include avian apovery low density lipoprotein II mRNA (8), vitellogenin (9), transferrin receptor mRNA (10), ␤-globin mRNA (11,12), insulin-like growth factor II mRNA (13), and Xenopus serum albumin mRNA (14). On a functional level endonuclease cleavage within the mRNA body has the same effect as deadenylation in that it disrupts the physical relationship between the cap and the poly(A) tail.…”

mentioning

confidence: 99%

Endonuclease-mediated mRNA Decay Requires Tyrosine Phosphorylation of Polysomal Ribonuclease 1 (PMR1) for the Targeting and Degradation of Polyribosome-bound Substrate mRNA

Yang

Peng²,

Schoenberg

2004

Journal of Biological Chemistry

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PMR1 is an endonuclease that is activated by estrogen to degrade Xenopus albumin mRNA. A previous report showed that the functional unit of endonuclease-mediated mRNA decay is a ϳ680-kDa polysome-bound complex that contains both PMR1 and substrate mRNA. PMR1 contains two domains involved in endonuclease targeting to polysomes, an N-terminal domain that lies between residues 200 and 250, and a C-terminal domain that lies within the last 100 residues. Loss of either domain inactivated PMR1 targeting to polysomes and stabilized albumin mRNA. The current study identified a phosphorylated tyrosine residue within the C-terminal polysome-targeting domain and showed that this modification is required for PMR1-mediated mRNA decay. Changing this tyrosine to phenylalanine inactivated the targeting of PMR1 to polysomes, blocked binding of PMR1 to the functional complex containing its substrate mRNA, prevented the targeting of a green fluorescent protein fusion protein to this complex, and stabilized albumin mRNA to degradation by PMR1 in vivo. A general tyrosine kinase inhibitor inhibited the phosphorylation of PMR1, which in turn inhibited PMR1-catalyzed degradation of albumin mRNA. These results indicate that one or more tyrosine kinases functions as a regulator of endonuclease-mediated mRNA decay.

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“…For vigilin overexpression, pTetCMV-Fo(AS)-vigilin (Cunningham et al, 2000) was transfected using Fugene HD (Roche). The BT20 cells at 75-80% confluence in 6-well plates were transfected with 5 g of plasmids.…”

Section: Gain-of-function and Loss-of-function Assaymentioning

confidence: 99%

Post-Transcriptional Regulation of Proto-Oncogene c-fms in Breast Cancer

Woo¹,

Chambers²

2013

Oncogene and Cancer - From Bench to Clinic

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Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3′-untranslated region by the mRNA endonuclease polysomal ribonuclease 1

Cited by 77 publications

References 27 publications

Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner

Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner

Endonuclease-mediated mRNA Decay Requires Tyrosine Phosphorylation of Polysomal Ribonuclease 1 (PMR1) for the Targeting and Degradation of Polyribosome-bound Substrate mRNA

Post-Transcriptional Regulation of Proto-Oncogene c-fms in Breast Cancer

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