Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-9-2
pubmed:databankReference
pubmed:abstractText
By differential screening of a cDNA library obtained from a GM-CSF-dependent human myeloid leukemia cell line (GF-D8), we identified two novel isoforms of the recently described ZNF162 gene, which is apparently linked to multiple endocrine neoplasia type 1. The shorter of these new isoforms, called B3, presents an open reading frame (ORF) of 1713 bp coding for 571 amino acids. Its nucleotide sequence is homologous to the cDNA coding for the ABCDF isoform of ZNF162, except for a 4-nucleotide insertion that results in a frame shift of the ORF starting from nucleotide 1725 of the ZNF162 sequence. As a consequence, the predicted translation product of B3 contains the consensus sequence of the A motif (G-X-X-X-X-G-K-S) of the "ATP/ GTP binding site," which is characteristic of several protein families including protein kinases. Moreover, B3 shows the use of a different stop codon and contains a different tyrosine-rich COOH terminus. The longer isoform, called B4, differs from the ABCDEF isoform of ZNF162 by the insertion, at position 2137, of 383 nucleotides leading to a different, proline-rich COOH terminus. The complex transcription pattern of the ZNF162 gene is characterized by four transcripts, of approximately 3.9, 3.7, 3.2, and 2.9 kb, in GF-D8 cells. The 3.7- and 2.9-kb transcripts are expressed in resting GF-D8 cells. Upon stimulation with GM-CSF the expression of these mRNAs is up-regulated in parallel with the induction of two additional transcripts of 3.9 and 3.2 kb. The same pattern of expression has also been observed in freshly isolated myeloid leukemia cells and normal CD34+ stem cells. In light of these data, and since GM-CSF is known to stimulate signal transduction pathways, it becomes relevant that all the different isoforms of ZNF162 contain the KH module, which is a sequence motif present in proteins playing a major role in regulating cellular RNA metabolism. A search for functional domains demonstrates that ZNF162 belongs to a new and growing family of genes dubbed STAR (signal transduction and activator of RNA) proteins that are thought to play a downstream role in cell signaling and also in RNA binding. The mammalian members include Sam68, which is a target of Src, Fyn, and Grb2, and the newly cloned mouse quaking proteins (qkI) necessary in early embryogenesis and myelination. Moreover, since ZNF162 is highly conserved from yeast to humans, it implies that this new pathway has a significant function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0888-7543
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
268-77
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:9192847-Amino Acid Sequence, pubmed-meshheading:9192847-Animals, pubmed-meshheading:9192847-Base Sequence, pubmed-meshheading:9192847-Consensus Sequence, pubmed-meshheading:9192847-DNA, Complementary, pubmed-meshheading:9192847-DNA Primers, pubmed-meshheading:9192847-DNA-Binding Proteins, pubmed-meshheading:9192847-Gene Expression Regulation, pubmed-meshheading:9192847-Genes, pubmed-meshheading:9192847-Granulocyte-Macrophage Colony-Stimulating Factor, pubmed-meshheading:9192847-Humans, pubmed-meshheading:9192847-Leukemia, Myeloid, Acute, pubmed-meshheading:9192847-Mice, pubmed-meshheading:9192847-Molecular Sequence Data, pubmed-meshheading:9192847-Polymerase Chain Reaction, pubmed-meshheading:9192847-RNA, pubmed-meshheading:9192847-Sequence Homology, Amino Acid, pubmed-meshheading:9192847-Signal Transduction, pubmed-meshheading:9192847-Transcription Factors, pubmed-meshheading:9192847-Tumor Cells, Cultured, pubmed-meshheading:9192847-Zinc Fingers
pubmed:year
1997
pubmed:articleTitle
Identification of two novel isoforms of the ZNF162 gene: a growing family of signal transduction and activator of RNA proteins.
pubmed:affiliation
Divisione di Ematologia, Ospedali Riuniti di Bergamo, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't