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The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies

Article Abstract:

The p23 molecular chaperones participate in a step late in intracellular receptor activity to affect ligand efficacies differentially. Effects of three p23 proteins on IR activities have been compared. They were yeast p23, and the two human p23 homologs, p23 and tsp23. This work seems to resolve what appear to be discrepancies in earlier reports on the role of p23 on steroid receptor function.

Author: Freeman, Brian C., Felts, Sara J., Toft, David O., Yamamoto, Keith R.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2000
Proteins, Steroid hormones, Steroid receptors

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Regulation of DAF-2 receptor signaling by human insulin and ins-1, a member of the unusually large and diverse C. elegans insulin gene family

Article Abstract:

A member of the unusually large and diverse Caenorhabditis elegans insulin gene family is discussed relative to regulation of DAF-2 receptor signaling. Both human insulin and ins-1, the gene, are involved in the regulation. The insulin superfamily in humans/vertebrates may be much more extensive than has been believed. A systematic search of the genome sequence of C. elegans for genes that encode members of the insulin superfamily is described.

Author: Ruvkun, Gary, Pierce, Sarah B., Costa, Michael, Wisotzkey, Robert, Devadhar, Sharmila, Homburger, Sheila A., Buchman, Andrew R., Ferguson, Kimberly C., Heller, Jonathan, Platt, Darren M., Pasquinelli, Amy A., Liu, Leo X., Doberstein, Stephen K.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2001
Statistical Data Included, Genetic aspects, Cellular signal transduction, Insulin, Life spans (Biology)

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Structure and specificity of nuclear receptor-coactivator interactions

Article Abstract:

Amphipathic helices interact with hydrophobic grooves may permit flexibility in protein combinational regulation, while side chains at interfaces provide for specificity. Hormone binding, when examined through biochemical and crystallographic analyses, forms hydrophobic grooves inside the ligand binding domain of the thyroid hormone receptor. Regulation of transcription requires precise assembly of multiprotein regulatory complexes, and this research has suggested one means by which this is accomplished.

Author: Yamamoto, Keith R., Fletterick, Robert J., Baxter, John D., Stallcup, Michael R., Wagner, Richard L., Apriletti, James W., Darimont, Beatrice D., Kushner, Peter J.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
Analysis, Cell research, Cytological research, Genetic research

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Subjects list: Research, United States, Physiological aspects, Cytochemistry, Ligands (Biochemistry), Cell receptors
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