NDLI: Selective Regulation of MAP Kinase Signaling by an Endomembrane Phosphatidylinositol 4-Kinase*

Content Provider	PubMed Central
Author	Cappell, Steven D. Dohlman, Henrik G.
Abstract	Multiple MAP kinase pathways share components yet initiate distinct biological processes. Signaling fidelity can be maintained by scaffold proteins and restriction of signaling complexes to discreet subcellular locations. For example, the yeast MAP kinase scaffold Ste5 binds to phospholipids produced at the plasma membrane and promotes selective MAP kinase activation. Here we show that Pik1, a phosphatidylinositol 4-kinase that localizes primarily to the Golgi, also regulates MAP kinase specificity but does so independently of Ste5. Pik1 is required for full activation of the MAP kinases Fus3 and Hog1 and represses activation of Kss1. Further, we show by genetic epistasis analysis that Pik1 likely regulates Ste11 and Ste50, components shared by all three MAP kinase pathways, through their interaction with the scaffold protein Opy2. These findings reveal a new regulator of signaling specificity functioning at endomembranes rather than at the plasma membrane.
Related Links	http://dx.doi.org/10.1074/jbc.m110.195073
Ending Page	14860
Page Count	9
Starting Page	14852
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	17
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-04-29
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Selective Regulation of MAP Kinase Signaling by an Endomembrane Phosphatidylinositol 4-Kinase

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Selective Regulation of MAP Kinase Signaling by an Endomembrane Phosphatidylinositol 4-Kinase

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