scholarly journals Functional Significance of the Interaction between the mRNA-binding Protein, Nab2, and the Nuclear Pore-associated Protein, Mlp1, in mRNA Export

2008 ◽  
Vol 283 (40) ◽  
pp. 27130-27143 ◽  
Author(s):  
Milo B. Fasken ◽  
Murray Stewart ◽  
Anita H. Corbett
Keyword(s):  
Functional Significance ◽  
Binding Protein ◽  
Mrna Export ◽  
Nuclear Pore ◽  
Mrna Binding Protein ◽  
Mrna Binding

scholarly journals A Distinct and Parallel Pathway for the Nuclear Import of an mRNA-binding Protein

1997 ◽  
Vol 139 (7) ◽  
pp. 1645-1653 ◽  
Author(s):  
Lucy F. Pemberton ◽  
Jonathan S. Rosenblum ◽  
Günter Blobel
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Import ◽  
Binding Protein ◽  
Nuclear Pore ◽  
Polyadenylated Rna ◽  
Mrna Binding Protein ◽  
Parallel Pathway ◽  
Rna Export ◽  
Mrna Binding ◽  
Transport Factors

Three independent pathways of nuclear import have so far been identified in yeast, each mediated by cognate nuclear transport factors, or karyopherins. Here we have characterized a new pathway to the nucleus, mediated by Mtr10p, a protein first identified in a screen for strains defective in polyadenylated RNA export. Mtr10p is shown to be responsible for the nuclear import of the shuttling mRNA-binding protein Npl3p. A complex of Mtr10p and Npl3p was detected in cytosol, and deletion of Mtr10p was shown to lead to the mislocalization of nuclear Npl3p to the cytoplasm, correlating with a block in import. Mtr10p bound peptide repeat-containing nucleoporins and Ran, suggesting that this import pathway involves a docking step at the nuclear pore complex and is Ran dependent. This pathway of Npl3p import is distinct and does not appear to overlap with another known import pathway for an mRNA-binding protein. Thus, at least two parallel pathways function in the import of mRNA-binding proteins, suggesting the need for the coordination of these pathways.

scholarly journals Hypoxia up-regulates the activity of a novel erythropoietin mRNA binding protein.

1991 ◽  
Vol 266 (25) ◽  
pp. 16594-16598
Author(s):  
I.J. Rondon ◽  
L.A. MacMillan ◽  
B.S. Beckman ◽  
M.A. Goldberg ◽  
T. Schneider ◽  
...  
Keyword(s):  
Binding Protein ◽  
Mrna Binding Protein ◽  
Mrna Binding

Increased expression of the MBP mRNA binding protein HnRNP A2 during oligodendrocyte differentiation

2004 ◽  
Vol 75 (5) ◽  
pp. 614-623 ◽  
Author(s):  
M. Maggipinto ◽  
C. Rabiner ◽  
G.J. Kidd ◽  
A.J. Hawkins ◽  
R. Smith ◽  
...  
Keyword(s):  
Binding Protein ◽  
Oligodendrocyte Differentiation ◽  
Mrna Binding Protein ◽  
Mrna Binding

scholarly journals Human Insulin Growth Factor 2 mRNA Binding Protein 2 Increases MicroRNA 33a/b Inhibition of Liver ABCA1 Expression and Alters Low-Density Apolipoprotein Levels in Mice

2020 ◽  
Vol 40 (16) ◽  
Author(s):  
Muhua Yang ◽  
Christina Gallo-Ebert ◽  
Michael Hayward ◽  
Weidong Liu ◽  
Virginia McDonough ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Association Studies ◽  
Blood Levels ◽  
Genome Wide Association Studies ◽  
Low Density ◽  
Nucleotide Polymorphisms ◽  
Insulin Growth Factor ◽  
Mrna Binding Protein ◽  
Mrna Binding

ABSTRACT Genome-wide association studies (GWAS) have linked IGF2BP2 single-nucleotide polymorphisms (SNPs) with type 2 diabetes (T2D). Mice overexpressing mIGF2BP2 have elevated cholesterol levels when fed a diet that induces hepatic steatosis. These and other studies suggest an important role for insulin growth factor 2 mRNA binding protein 2 (IGF2BP2) in the initiation and progression of several metabolic disorders. The ATPase binding cassette protein ABCA1 initiates nascent high-density apolipoprotein (HDL) biogenesis by transferring phospholipid and cholesterol to delipidated apolipoprotein AI (ApoAI). Individuals with mutational ablation of ABCA1 have Tangier disease, which is characterized by a complete loss of HDL. MicroRNA 33a and 33b (miR-33a/b) bind to the 3′ untranslated region (UTR) of ABCA1 and repress its posttranscriptional gene expression. Here, we show that IGF2BP2 works together with miR-33a/b in repressing ABCA1 expression. Our data suggest that IGF2BP2 is an accessory protein of the argonaute (AGO2)–miR-33a/b–RISC complex, as it directly binds to miR-33a/b, AGO2, and the 3′ UTR of ABCA1. Finally, we show that mice overexpressing human IGF2BP2 have decreased ABCA1 expression, increased low-density lipoprotein-cholesterol (LDL-C) and cholesterol blood levels, and elevated SREBP-dependent signaling. Our data support the hypothesis that IGF2BP2 has an important role in maintaining lipid homeostasis through its modulation of ABCA1 expression, as its overexpression or loss leads to dyslipidemia.

scholarly journals The mRNA-binding protein IGF2BP1 maintains intestinal barrier function by up-regulating occludin expression

2020 ◽  
Vol 295 (25) ◽  
pp. 8602-8612
Author(s):  
Vikash Singh ◽  
Chethana P. Gowda ◽  
Vishal Singh ◽  
Ashwinkumar S. Ganapathy ◽  
Dipti M. Karamchandani ◽  
...  
Keyword(s):  
Intestinal Epithelium ◽  
Barrier Function ◽  
Binding Protein ◽  
Intestinal Barrier ◽  
Intestinal Barrier Function ◽  
Intestinal Epithelial ◽  
Adult Mice ◽  
Junction Protein ◽  
Mrna Binding Protein ◽  
Mrna Binding

Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) is an mRNA-binding protein that has an oncofetal pattern of expression. It is also expressed in intestinal tissue, suggesting that it has a possible role in intestinal homeostasis. To investigate this possibility, here we generated Villin CreERT2:Igf2bp1flox/flox mice, which enabled induction of an IGF2BP1 knockout specifically in intestinal epithelial cells (IECs) of adult mice. Using gut barrier and epithelial permeability assays and several biochemical approaches, we found that IGF2BP1 ablation in the adult intestinal epithelium causes mild active colitis and mild-to-moderate active enteritis. Moreover, the IGF2BP1 deletion aggravated dextran sodium sulfate–induced colitis. We also found that IGF2BP1 removal compromises barrier function of the intestinal epithelium, resulting from altered protein expression at tight junctions. Mechanistically, IGF2BP1 interacted with the mRNA of the tight-junction protein occludin (Ocln), stabilizing Ocln mRNA and inducing expression of occludin in IECs. Furthermore, ectopic occludin expression in IGF2BP1-knockdown cells restored barrier function. We conclude that IGF2BP1-dependent regulation of occludin expression is an important mechanism in intestinal barrier function maintenance and in the prevention of colitis.

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