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report on a novel homozygous HSF4 mutation (c.521T>C, p.Leu174Pro) in two sibs with congenital cataracts
BCAS2 (show BCAS2 Proteins) interacts with HSF4 and negatively regulates its protein stability via ubiquitination.
HSF4 may work as a switch between lens epithelial cell proliferation and secondary fiber cell differentiation, a process which mainly depends on p53 (show TP53 Proteins).
Nuclear HSF2 and HSF4 bound to HSF1 (show HSF1 Proteins) only after heat shock.
concluded that the new mutation of c.331C>T in HSF4 DNA may be responsible for the autosomal dominant congenital cataract in this family
We found that HSF4 downregulation led to decrease of HIF1alpha (show HIF1A Proteins) mRNA expression
HSF4 p.Arg116His recreates the childhood lamellar cataract in mice suggesting that incomplete penetrance associated with early cataracts may not be an absence but a limitation of the detection of the phenotype
This is the first report of the novel missense mutation, c.69 G-->T (p. K23N), in exon 3 of the HSF4 locus on 16q21-q22 associated with bilateral congenital cataracts in a Chinese family.
the transcriptional activation of HSF4 is mediated by interactions between activator and repressor domains within the C-terminal end.
This comparative analysis with CRYAB (show CRYAB Proteins) and HSP70 (show HSP70 Proteins) demonstrates that differential heat shock response is controlled by cell-type-dependent access of HSF1 (show HSF1 Proteins) and HSF4 to specific promoters, independent of the promoter architecture.
a novel molecular mechanism of HSF4 in regulating lens epithelial cell homeostasis
The deletion of Hsf4 affects the expression of many genes, such as Ubc, Ptgs2, Egr1 and Fos. These genes may be involved in the development of cataract.
A novel regulatory mechanism between Hsf1 (show HSF1 Proteins) and Hsf4b in modulating lens epithelial cell homeostasis.
Mutations in the DNA binding domain (DBD) of the heat shock transcription factor 4 (HSF4) are known to be associated with early childhood autosomal dominant lamellar cataract.
Hsf4b is a novel downstream transcription factor of FGF2 (show FGF2 Proteins), and its transcription activity is associated with FGF2 (show FGF2 Proteins)-modulated lens epithelial cell-fiber cell transition.
These results revealed an essential role for HSF4-mediated SKAP2 expression in the regulation of actin reorganization during lens differentiation.
Data reveal the lens-specific role of heat shock transcription factor 4 (HSF4), and indicate that HSF1 (show HSF1 Proteins) and HSF4 are involved in regulating expression of growth factor genes.
HSF4 fulfills a central role in controlling spatial and temporal expression of genes critical for correct development and function of the lens.
Heat-shock transcription factors (HSFs) activate heat-shock response genes under conditions of heat or other stresses. HSF4 lacks the carboxyl-terminal hydrophobic repeat which is shared among all vertebrate HSFs and has been suggested to be involved in the negative regulation of DNA binding activity. Two alternatively spliced transcripts encoding distinct isoforms and possessing different transcriptional activity have been described.
, HSTF 4
, heat shock factor protein 4
, DNA binding protein
, binds heat shock DNA elements
, heat shock factor 4
, heat shock transcription factor 4 variant a
, heat shock transcription factor 4 variant b
, heat shock transcription factor 4 variant c