Activation of erythropoietin signaling by receptor dimerization

Stephanie S. Watowich

doi:10.1016/S1357-2725(99)00075-8

Activation of erythropoietin signaling by receptor dimerization

Stephanie S. Watowich

Immunology

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

The hormone erythropoietin (Epo) is essential for red blood cell development. Epo binds a high affinity receptor on the surface of erythroid progenitor cells, stimulating receptor dimerization and activation of the intracellular signal transduction pathways that support erythroid cell survival, proliferation and differentiation. Biochemical and structural analysis of the erythropoietin receptor (EpoR) is revealing the molecular mechanisms of EpoR function, leading the way to the development of small molecule Epo mimetics. This review focuses on the role EpoR dimerization plays in receptor function. Copyright (C) 1999.

Original language	English (US)
Pages (from-to)	1075-1088
Number of pages	14
Journal	International Journal of Biochemistry and Cell Biology
Volume	31
Issue number	10
DOIs	https://doi.org/10.1016/S1357-2725(99)00075-8
State	Published - Oct 1999

Keywords

Epo mimetics
EpoR dimerization
EpoR function
EpoR structure
Erythropoiesis

ASJC Scopus subject areas

Biochemistry
Cell Biology

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10.1016/S1357-2725(99)00075-8

Cite this

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title = "Activation of erythropoietin signaling by receptor dimerization",

abstract = "The hormone erythropoietin (Epo) is essential for red blood cell development. Epo binds a high affinity receptor on the surface of erythroid progenitor cells, stimulating receptor dimerization and activation of the intracellular signal transduction pathways that support erythroid cell survival, proliferation and differentiation. Biochemical and structural analysis of the erythropoietin receptor (EpoR) is revealing the molecular mechanisms of EpoR function, leading the way to the development of small molecule Epo mimetics. This review focuses on the role EpoR dimerization plays in receptor function. Copyright (C) 1999.",

keywords = "Epo mimetics, EpoR dimerization, EpoR function, EpoR structure, Erythropoiesis",

author = "Watowich, {Stephanie S.}",

note = "Funding Information: I thank Stan Watowich and Bob Stroud for discussions and for providing insight into the EpoBP structures, Bob Stroud for assistance and permission to reproduce Fig. 2 , and Stan Watowich for providing the image in Fig. 3 and for critical review of the manuscript. Work in my laboratory is supported by grants from the National Institutes of Health, the Texas Higher Education Coordinating Board, and the Gillson-Longenbaugh Foundation.",

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T1 - Activation of erythropoietin signaling by receptor dimerization

AU - Watowich, Stephanie S.

N1 - Funding Information: I thank Stan Watowich and Bob Stroud for discussions and for providing insight into the EpoBP structures, Bob Stroud for assistance and permission to reproduce Fig. 2 , and Stan Watowich for providing the image in Fig. 3 and for critical review of the manuscript. Work in my laboratory is supported by grants from the National Institutes of Health, the Texas Higher Education Coordinating Board, and the Gillson-Longenbaugh Foundation.

PY - 1999/10

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N2 - The hormone erythropoietin (Epo) is essential for red blood cell development. Epo binds a high affinity receptor on the surface of erythroid progenitor cells, stimulating receptor dimerization and activation of the intracellular signal transduction pathways that support erythroid cell survival, proliferation and differentiation. Biochemical and structural analysis of the erythropoietin receptor (EpoR) is revealing the molecular mechanisms of EpoR function, leading the way to the development of small molecule Epo mimetics. This review focuses on the role EpoR dimerization plays in receptor function. Copyright (C) 1999.

AB - The hormone erythropoietin (Epo) is essential for red blood cell development. Epo binds a high affinity receptor on the surface of erythroid progenitor cells, stimulating receptor dimerization and activation of the intracellular signal transduction pathways that support erythroid cell survival, proliferation and differentiation. Biochemical and structural analysis of the erythropoietin receptor (EpoR) is revealing the molecular mechanisms of EpoR function, leading the way to the development of small molecule Epo mimetics. This review focuses on the role EpoR dimerization plays in receptor function. Copyright (C) 1999.

KW - Epo mimetics

KW - EpoR dimerization

KW - EpoR function

KW - EpoR structure

KW - Erythropoiesis

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ER -

Activation of erythropoietin signaling by receptor dimerization

Abstract

Keywords

ASJC Scopus subject areas

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