A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development
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A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development. / Nielsen, J; Christiansen, J; Lykke-Andersen, J; Johnsen, A H; Wewer, Ulla M.; Nielsen, F C.
In: Molecular and Cellular Biology, Vol. 19, No. 2, 1999, p. 1262-1270.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development
AU - Nielsen, J
AU - Christiansen, J
AU - Lykke-Andersen, J
AU - Johnsen, A H
AU - Wewer, Ulla M.
AU - Nielsen, F C
PY - 1999
Y1 - 1999
N2 - Insulin-like growth factor II (IGF-II) is a major fetal growth factor. The IGF-II gene generates multiple mRNAs with different 5' untranslated regions (5' UTRs) that are translated in a differential manner during development. We have identified a human family of three IGF-II mRNA-binding proteins (IMPs) that exhibit multiple attachments to the 5' UTR from the translationally regulated IGF-II leader 3 mRNA but are unable to bind to the 5' UTR from the constitutively translated IGF-II leader 4 mRNA. IMPs contain the unique combination of two RNA recognition motifs and four hnRNP K homology domains and are homologous to the Xenopus Vera and chicken zipcode-binding proteins. IMP localizes to subcytoplasmic domains in a growth-dependent and cell-specific manner and causes a dose-dependent translational repression of IGF-II leader 3 -luciferase mRNA. Mouse IMPs are produced in a burst at embryonic day 12.5 followed by a decline towards birth, and, similar to IGF-II, IMPs are especially expressed in developing epithelia, muscle, and placenta in both mouse and human embryos. The results imply that cytoplasmic 5' UTR-binding proteins control IGF-II biosynthesis during late mammalian development.
AB - Insulin-like growth factor II (IGF-II) is a major fetal growth factor. The IGF-II gene generates multiple mRNAs with different 5' untranslated regions (5' UTRs) that are translated in a differential manner during development. We have identified a human family of three IGF-II mRNA-binding proteins (IMPs) that exhibit multiple attachments to the 5' UTR from the translationally regulated IGF-II leader 3 mRNA but are unable to bind to the 5' UTR from the constitutively translated IGF-II leader 4 mRNA. IMPs contain the unique combination of two RNA recognition motifs and four hnRNP K homology domains and are homologous to the Xenopus Vera and chicken zipcode-binding proteins. IMP localizes to subcytoplasmic domains in a growth-dependent and cell-specific manner and causes a dose-dependent translational repression of IGF-II leader 3 -luciferase mRNA. Mouse IMPs are produced in a burst at embryonic day 12.5 followed by a decline towards birth, and, similar to IGF-II, IMPs are especially expressed in developing epithelia, muscle, and placenta in both mouse and human embryos. The results imply that cytoplasmic 5' UTR-binding proteins control IGF-II biosynthesis during late mammalian development.
KW - 3T3 Cells
KW - Amino Acid Sequence
KW - Animals
KW - Binding Sites
KW - Cell Line
KW - Chickens
KW - Cloning, Molecular
KW - DNA, Complementary
KW - Embryonic and Fetal Development
KW - Gene Expression Regulation, Developmental
KW - Humans
KW - Insulin-Like Growth Factor II
KW - Mice
KW - Molecular Sequence Data
KW - Protein Biosynthesis
KW - RNA, Messenger
KW - RNA-Binding Proteins
KW - Sequence Homology, Amino Acid
KW - Xenopus
M3 - Journal article
C2 - 9891060
VL - 19
SP - 1262
EP - 1270
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
SN - 0270-7306
IS - 2
ER -
ID: 191547