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MIF4GD encodes a protein which interacts with the N-terminus of the stem-loop binding protein (SLBP) and the 3' end of histone mRNA.
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Results suggest that MIF4GD is a potential regulator of p27 (show PAK2 Proteins)-dependent cell proliferation in HCC (show FAM126A Proteins).
This paper describes the oligomeric state of SLIP1 and the SLIP1-SLBP (show SLBP Proteins) complex and how it is regulated by SLBP (show SLBP Proteins) phosphorylation. Using alanine scanning mutagenesis, the authors demonstrate that the binding site on SLIP1 for SLBP (show SLBP Proteins) lies close to the dimer interface. A single-point mutant near the SLIP1 homodimer interface abolished interaction with SLBP (show SLBP Proteins) in vitro and reduced the abundance of histone mRNA in vivo.
INT6 (show EIF3E Proteins) and MIF4GD were observed to colocalize in cytoplasmic foci. It was concluded that INT6 (show EIF3E Proteins), by establishing interactions with MIF4GD and SLBP (show SLBP Proteins), plays an important role in translation of poly(A) minus histone mRNAs.
downregulation of endogenous SLIP1 reduces the rate of translation of endogenous histone mRNA and also reduces cell viability.
This gene encodes a protein which interacts with the N-terminus of the stem-loop binding protein (SLBP) and the 3' end of histone mRNA. This interaction facilitates the activation of histone mRNA translation. Alternative splicing results in multiple transcript variants encoding different isoforms.
MIF4G domain containing
, MIF4G domain-containing protein
, SLBP (stem loop binding protein)-interacting protein 1
, SLBP-interacting protein 1