NDLI: The Na+/H+ Exchanger Regulatory Factor Stabilizes Epidermal Growth Factor Receptors at the Cell Surface

Content Provider	PubMed Central
Author	Lazar, Cheri S. Cresson, Catherine M. Lauffenburger, Douglas A. Gill, Gordon N.
Editor	Juan, S. Bonifacino
Copyright Year	2004
Abstract	Ligand binding to cell surface receptors initiates both signal transduction and endocytosis. Although signaling may continue within the endocytic compartment, down-regulation is the major mechanism that controls the concentration of cell surface receptors, their ability to receive environmental signals, and the ultimate strength of biological signaling. Internalization, recycling, and trafficking of receptor tyrosine kinases (RTKs) within the endosome compartment are each regulated to control the overall process of down-regulation. We have identified the Na+/H+ exchanger regulatory factor (NHERF) as an important molecular component that stabilizes epidermal growth factor receptors (EGFRs) at the cell surface to restrict receptor down-regulation. The NH2-terminal PDZ domain (PDZ 1) of NHERF specifically binds to an internal peptide motif located within the COOH-terminal regulatory domain of EGFR. Expression of NHERF slows the rate of EGF-induced receptor degradation. A point mutation that abolishes the PDZ 1 recognition sequence of EGFR enhances the rate of ligand-induced endocytosis and down-regulation of EGFR. Similarly, expression of a dominant negative mutant of NHERF enhances EGF-induced receptor down-regulation. In contrast to β-adrenergic receptors where NHERF enhances recycling of internalized receptors, NHERF stabilizes EGFR at the cell surface and slows the rate of endocytosis without affecting recycling. Although the mechanisms differ, for both RTKs and G protein-coupled receptors, the overall effect of NHERF is to enhance the fraction of receptors present at the cell surface.
Related Links	http://dx.doi.org/10.1091/mbc.e04-03-0239
Ending Page	5480
Page Count	11
Starting Page	5470
File Format	PDF
ISSN	10591524
Journal	Molecular Biology of the Cell
Issue Number	12
Volume Number	15
Language	English
Publisher	The American Society for Cell Biology
Publisher Date	2004-09-01
Access Restriction	Open
Rights Holder	The American Society for Cell Biology
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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Platelet-Derived Growth Factor Receptor Association with Na+/H+ Exchanger Regulatory Factor Potentiates Receptor Activity

Structural Determinants of the Na+/H+Exchanger Regulatory Factor Interaction with the β2Adrenergic and Platelet-derived Growth Factor Receptors

Ligand-induced recruitment of Na+/H+-exchanger regulatory factor to the PDGF (platelet-derived growth factor) receptor regulates actin cytoskeleton reorganization by PDGF.

Na+/H+ Exchanger Regulatory Factor 1 (NHERF1) Directly Regulates Osteogenesis*

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Lysophosphatidic acid 5 receptor induces activation of Na+/H+ exchanger 3 via apical epidermal growth factor receptor in intestinal epithelial cells

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Expression of Na+/H+ exchanger regulatory factor 1 in autosomal-dominant polycystic kidney disease

Structure of the 5'-flanking regulatory region and gene for the human growth factor-activatable Na/H exchanger NHE-1.

The Na+/H+ Exchanger Regulatory Factor Stabilizes Epidermal Growth Factor Receptors at the Cell Surface

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Ligand-induced recruitment of Na+/H+-exchanger regulatory factor to the PDGF (platelet-derived growth factor) receptor regulates actin cytoskeleton reorganization by PDGF.

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The Na+/H+ Exchanger Regulatory Factor Stabilizes Epidermal Growth Factor Receptors at the Cell Surface