Structural Characterization of the Stem–Stem Dimerization Interface between Prolactin Receptor Chains Complexed with the Natural Hormone

Agthoven, Jan van; Zhang, Chi; Tallet, Estelle; Raynal, Bertrand; Hoos, Sylviane; Baron, Bruno; England, Patrick; Goffin, Vincent; Broutin, Isabelle

doi:10.1016/j.jmb.2010.09.036

Cited by 46 publications

(47 citation statements)

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“…In the ternary PRL⅐receptor complex (Fig. 1B), Trp-124 is only involved in the receptor interface from PRLR2 (25); therefore, it is likely that the regulatory mechanism involving the residue quartet only applies to that receptor.…”

Section: Discussionmentioning

confidence: 99%

“…The spectra were phased on the direct dimension and analyzed in CcpNmr analysis using the assignment of hPRLR-D2 (BMRB accession code 17752 (15)) as a starting point. Changes in chemical shifts obtained Surface Plasmon Resonance-rPRLR-ECD WT and rPRLR-ECD L170F were immobilized covalently onto nitrilotriacetic acid-derivatized sensor chips, as described (23)(24)(25). Surface densities of 3,000 -4,000 resonance units (resonance unit Ϸ pg mm Ϫ2 ) were obtained.…”

Section: Methodsmentioning

confidence: 99%

“…1B) (25). To investigate the role of these inter-molecular contacts for signal transfer, alanine substitutions were generated in the full-length receptor (rPRLR K168A and rPRLR F170A ), and their capacity to activate the canonical STAT5 pathway in transiently transfected HEK293 fibroblasts was analyzed ( Fig.…”

Section: Prlr Interface Residues Control Signaling Selectivity-usingmentioning

confidence: 99%

“…Previously, the overall fold of the rPRLR-ECD interface variants (K168A and F170A) were evaluated from their far-UV circular dichroism (CD) spectra (25). Because of the presence of aromatic residues that are spatially close to each other in the ECD, this gives rise to a through-space coupling of their electric dipoles.…”

Section: Residue 170 Directs the Prlr Species-specific Signaling Profmentioning

confidence: 99%

“…PRLR homodimer interface (site 3). A, representation of the 2:1 rPRLR⅐hPRL complex structure (PDB accession code 3NPZ) (25). The two receptors (rPRLR1 and rPRLR2) are shown in gray, and their D1 and D2 domains are labeled in light and dark blue, respectively, and hPRL is shown in pale cyan.…”

mentioning

confidence: 99%

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A Residue Quartet in the Extracellular Domain of the Prolactin Receptor Selectively Controls Mitogen-activated Protein Kinase Signaling

Zhang¹,

Nygaard²,

Haxholm³

et al. 2015

Journal of Biological Chemistry

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Background: Discrimination of cytokine receptor signaling pathways is poorly understood. Results: Manipulation of extracellular prolactin receptor interface residues selectively affected activation of the MAPK pathway but not the STAT5 pathway. Conclusion: MAPK pathway activation correlated with apparent ligand⅐receptor complex lifetimes suggesting pathway-specific lifetime thresholds for activation. Significance: Discrimination of prolactin receptor signaling is controlled by the extracellular homodimer receptor interface.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Prlr Interface Residues Control Signaling Selectivity-usingmentioning

confidence: 99%

Section: Residue 170 Directs the Prlr Species-specific Signaling Profmentioning

confidence: 99%

mentioning

confidence: 99%

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A Residue Quartet in the Extracellular Domain of the Prolactin Receptor Selectively Controls Mitogen-activated Protein Kinase Signaling

Zhang¹,

Nygaard²,

Haxholm³

et al. 2015

Journal of Biological Chemistry

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Evolution of the Growth Hormone Receptor Family

Sheridan

2016

Encyclopedia of Life Sciences

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The growth hormone receptor (GHR) family includes receptors for growth hormone and prolactin receptor (PRLR). GHRs and PRLRs are membrane receptors that possess several evolutionarily conserved features: a hormone‐binding extracellular domain, a single‐chain transmembrane domain and an intracellular domain important for activating intracellular signal systems that mediate cell‐specific responses. PRLRs diverged early from a common GHR/PRLR in jawless fish (e.g. Agnathans), followed by subsequent divergence of GHRs in the Actinopterygian lineage that gave rise to teleosts and in the Sarcopterygian lineage that gave rise to tetrapods. Structural heterogeneity of GHRs in teleosts results from the existence of multiple genes that arose through a series of independent gene duplication events during the course of their evolution and from alternative transcripts of a single gene. Differential receptor–ligand interactions, differential receptor–cell signalling system interactions and the differential expression of alternate GHR forms underlie the vast array of functions elicited by GH. Key Concepts Growth hormone regulates many processes, including growth, metabolism, osmoregulation, reproduction and behaviour. Growth hormone receptors are single‐pass membrane‐bound receptors that mediate the actions of growth hormone. The growth hormone receptor family arose through a series of gene duplication events during the course of vertebrate evolution. The multiple actions of growth hormone arise from binding to variant forms of growth hormone receptor and from activation of alternate cell signalling pathways.

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A Century of Prolactin: Emerging Perspectives as a Metabolic Regulator

Wu,

Duan,

Jiang

et al. 2024

Diabetes Metabolism Res

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Prolactin, a hormone that has been studied for almost a century, has evolved from a reproductive regulator to a key player in metabolic health. Initially identified for its lactogenic role, the impact of prolactin on glucose and lipid metabolism became evident in the 1970s, leading to a paradigm shift in our understanding. Deviations in prolactin levels, including hyperprolactinaemia and hypoprolactinaemia, have been associated with adverse effects on glucose and lipid metabolism. Mechanistically, prolactin regulates metabolic homoeostasis by maintaining islet abundance, regulating the hypothalamic energy regulatory centre, balancing adipose tissue expansion, and regulating hepatic metabolism. Given the widespread use of pharmaceutical agents that affect prolactin levels, it is important to examine prolactin‐related metabolic effects. Recently, a profound exploration of the intricate metabolic role of prolactin has been conducted, encompassing its rhythm‐dependent regulatory influence on metabolism and its correlation with cognitive impairment associated with metabolic diseases. In this review, we highlight the role of prolactin as a metabolic regulator, summarise its metabolic effects, and discuss topics related to the association between prolactin and metabolic comorbidities.

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Structural Characterization of the Stem–Stem Dimerization Interface between Prolactin Receptor Chains Complexed with the Natural Hormone

Cited by 46 publications

References 46 publications

A Residue Quartet in the Extracellular Domain of the Prolactin Receptor Selectively Controls Mitogen-activated Protein Kinase Signaling

A Residue Quartet in the Extracellular Domain of the Prolactin Receptor Selectively Controls Mitogen-activated Protein Kinase Signaling

Evolution of the Growth Hormone Receptor Family

A Century of Prolactin: Emerging Perspectives as a Metabolic Regulator

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