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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Audhya, Anjon Weys, Sabine Stefan, Chris Emr, Scott D. Baird, Dan |
| Description | Author Affiliation: Baird D ( Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.) |
| Abstract | The phosphoinositide phosphatidylinositol 4-phosphate (PtdIns4P) is an essential signaling lipid that regulates secretion and polarization of the actin cytoskeleton. In Saccharomyces cerevisiae, the PtdIns 4-kinase Stt4 catalyzes the synthesis of PtdIns4P at the plasma membrane (PM). In this paper, we identify and characterize two novel regulatory components of the Stt4 kinase complex, Ypp1 and Efr3. The essential gene YPP1 encodes a conserved protein that colocalizes with Stt4 at cortical punctate structures and regulates the stability of this lipid kinase. Accordingly, Ypp1 interacts with distinct regions on Stt4 that are necessary for the assembly and recruitment of multiple copies of the kinase into phosphoinositide kinase (PIK) patches. We identify the membrane protein Efr3 as an additional component of Stt4 PIK patches. Efr3 is essential for assembly of both Ypp1 and Stt4 at PIK patches. We conclude that Ypp1 and Efr3 are required for the formation and architecture of Stt4 PIK patches and ultimately PM-based PtdIns4P signaling. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 6 |
| Volume Number | 183 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2008-12-15 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | 1-Phosphatidylinositol 4-Kinase Metabolism Adaptor Proteins, Vesicular Transport Cell Membrane Enzymology Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Cytology Cell Fractionation Gene Deletion Models, Biological Phosphatidylinositol Phosphates Protein Binding Protein Stability Protein Transport Chemistry Sequence Homology, Amino Acid Signal Transduction Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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