Expression of the hepatic specific V1 messenger ribonucleic acid of the human growth hormone receptor gene is regulated by hepatic nuclear factor (HNF)-4alpha2 and HNF-4alpha8.

Human (h) GH plays an essential role in growth and metabolism, and its effectiveness is modulated by the availability of its specific receptor [hGH receptor (hGHR)] on target cells. The hGHR gene has a complex 5'-regulatory region containing multiple first exons. Seven are clustered within two small regions: V2,V3,V9 (module A) and V1,V4,V7,V8 (module B).

Characterization of growth hormone receptor messenger ribonucleic acid variants in human adipocytes.

Context: Human GH exerts profound effects on adiposity through its specific receptor, hGHR. Eight hGHR mRNAs are produced by the hGHR gene due to splicing from alternate 5'-untranslated region first exons into a common acceptor site upstream of the start codon in exon 2. Four transcripts (V2, V3, V5, V9) are ubiquitously expressed, whereas the other four (V1, V4, V7, V8) are expressed only in normal postnatal liver, suggesting that different promoter usage is a mechanism for developmental- and tissue-specific regulation of the hGHR gene.

Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP.

The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface.