NDLI: Novel Phorbol Ester-binding Motif Mediates Hormonal Activation of Na+/H+ Exchanger

Content Provider	Journal of Biological Chemistry (JBC)
Author	Wakabayashi, Shigeo Nakamura, Tomoe Y. Kobayashi, Soushi Hisamitsu, Takashi
Abstract	Protein kinase C (PKC) is considered crucial for hormonal Na+/H+ exchanger (NHE1) activation because phorbol esters (PEs) strongly activate NHE1. However, here we report that rather than PKC, direct binding of PEs/diacylglycerol to the NHE1 lipid-interacting domain (LID) and the subsequent tighter association of LID with the plasma membrane mainly underlies NHE1 activation. We show that (i) PEs directly interact with the LID of NHE1 in vitro, (ii) like PKC, green fluorescent protein (GFP)-labeled LID translocates to the plasma membrane in response to PEs and receptor agonists, (iii) LID mutations markedly inhibit these interactions and PE/receptor agonist-induced NHE1 activation, and (iv) PKC inhibitors ineffectively block NHE1 activation, except staurosporin, which itself inhibits NHE1 via LID. Thus, we propose a PKC-independent mechanism of NHE1 regulation via a PE-binding motif previously unrecognized.
Related Links	http://www.jbc.org/content/285/34/26652.abstract
Ending Page	26661
Starting Page	26652
Page Count	10
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	34
Volume Number	285
DOI	10.1074/jbc.M110.130120
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2010-08-20
Access Restriction	Open
Subject Keyword	Cell pH Membrane Lipids Phorbol Esters Protein Kinase C (PKC) Sodium Proton Exchange Diacylglycerol Hormone Receptors Signal Transduction
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Novel Phorbol Ester-binding Motif Mediates Hormonal Activation of Na+/H+ Exchanger*

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Novel Phorbol Ester-binding Motif Mediates Hormonal Activation of Na+/H+ Exchanger

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