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Prolactin Receptor Signal Transduction

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Prolactin

Part of the book series: Endocrine Updates ((ENDO,volume 12))

Abstract

The pleiotropic actions of prolactin (PRL) are mediated by ligand-induced dimerization of its receptor, the PRLR. Structural analysis of the PRLR has revealed significant homology to other members of the cytokine receptor family, including the receptors for growth hormone (GH), erythropoietin, granulocyte-macrophage colony stimulating factor (GM-CSF) and interleukins 2-7 (1, 2). While the amino acid residues found within the extracellular domain of the PRLR are critical for its engagement of ligand, the structure of the PRLR intracellular domain also coordinates the interaction of several signaling networks, that orchestrate PRL induced gene expression (recent related overviews on this subject can be found in (3–6). It is the purpose of this chapter to examine the association and activation of these multimeric PRLR-associated signaling complexes at a molecular level. In doing so, several recently identified kinases, phosphatases, exchange factors, chaperones, isomerases, GTP-binding and adaptor/docking proteins will be overviewed. Finally, how these transduction networks act to mediate the specific signal initiated by PRL at both the genomic and non-genomic level will be discussed.

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  1. University of Pennsylvania Medical Center, Philadelphia, PA, USA

    Charles V. Clevenger, Michael A. Rycyzyn, Farhat Syed & J. Bradford Kline

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  1. Charles V. Clevenger
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  1. University of Cincinnati, USA

    Nelson D. Horseman

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Clevenger, C.V., Rycyzyn, M.A., Syed, F., Kline, J.B. (2001). Prolactin Receptor Signal Transduction. In: Horseman, N.D. (eds) Prolactin. Endocrine Updates, vol 12. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1683-5_18

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