Source:http://linkedlifedata.com/resource/pubmed/id/20081093
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rdf:type | |
lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0040624,
umls-concept:C0043457,
umls-concept:C0205245,
umls-concept:C0332120,
umls-concept:C0332597,
umls-concept:C0441655,
umls-concept:C0475264,
umls-concept:C0521447,
umls-concept:C1149301,
umls-concept:C1514562,
umls-concept:C1534709,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
6
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pubmed:dateCreated |
2010-6-2
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pubmed:abstractText |
Insulin-like growth factor binding protein (IGFBP)-5 is a secreted protein that binds to IGF and modulates IGF actions. IGFBP-5 is also found in the nucleus of mammalian cells and has transactivation activity. The structural basis of this transactivation activity and its role in mediating IGF-independent actions are not clear. Here we report that there are 2 igfbp-5 genes in zebrafish and other teleost fish. In zebrafish, igfbp-5a and -5b are expressed in spatially restricted, mostly nonoverlapping domains during early development. The IGF binding site is conserved in both zebrafish IGFBP-5s, and they are both secreted and capable of IGF binding. Both proteins contain a consensus bipartite nuclear localization signal and were found in the nucleus when introduced into cultured cells. Although zebrafish IGFBP-5b possesses transactivation activity, zebrafish IGFBP-5a lacks this activity. Mutational analysis demonstrated that 2 unique amino acids in positions 22 and 56 of IGFBP-5a are responsible for its lack of transactivation activity. These findings suggest that the duplicated zebrafish IGFBP-5s have evolved divergent regulatory mechanisms and distinct biological properties by partitioning of ancestral structural domains and provide new evidence for a conserved role of the IGF binding, nuclear localization, and transactivation domain of this multifunctional IGFBP.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1530-6860
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2020-9
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pubmed:meshHeading |
pubmed-meshheading:20081093-Amino Acid Sequence,
pubmed-meshheading:20081093-Animals,
pubmed-meshheading:20081093-Cell Nucleus,
pubmed-meshheading:20081093-Cloning, Molecular,
pubmed-meshheading:20081093-Cytoplasm,
pubmed-meshheading:20081093-Evolution, Molecular,
pubmed-meshheading:20081093-Genes, Duplicate,
pubmed-meshheading:20081093-In Situ Hybridization,
pubmed-meshheading:20081093-Insulin-Like Growth Factor Binding Protein 5,
pubmed-meshheading:20081093-Insulin-Like Growth Factor I,
pubmed-meshheading:20081093-Molecular Sequence Data,
pubmed-meshheading:20081093-Nuclear Localization Signals,
pubmed-meshheading:20081093-Phylogeny,
pubmed-meshheading:20081093-Protein Isoforms,
pubmed-meshheading:20081093-RNA, Messenger,
pubmed-meshheading:20081093-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:20081093-Sequence Homology, Amino Acid,
pubmed-meshheading:20081093-Transcriptional Activation,
pubmed-meshheading:20081093-Zebrafish
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pubmed:year |
2010
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pubmed:articleTitle |
Duplicated zebrafish insulin-like growth factor binding protein-5 genes with split functional domains: evidence for evolutionarily conserved IGF binding, nuclear localization, and transactivation activity.
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pubmed:affiliation |
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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