Yeast oxysterol-binding proteins: sterol transporters or regulators of cell polarization?
Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) are a conserved family of soluble cytoplasmic proteins that can bind sterols, translocate between membrane compartments, and affect sterol trafficking. These properties make ORPs attractive candidates for lipid transfer proteins (LTPs...
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| Veröffentlicht in: | Molecular and cellular biochemistry 2009-06, Vol.326 (1-2), p.9-13 |
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| creator | Beh, Christopher T Alfaro, Gabriel Duamel, Giselle Sullivan, David P Kersting, Michael C Dighe, Shubha Kozminski, Keith G Menon, Anant K |
| description | Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) are a conserved family of soluble cytoplasmic proteins that can bind sterols, translocate between membrane compartments, and affect sterol trafficking. These properties make ORPs attractive candidates for lipid transfer proteins (LTPs) that directly mediate nonvesicular sterol transfer to the plasma membrane. To test whether yeast ORPs (the Osh proteins) are sterol LTPs, we studied endoplasmic reticulum (ER)-to-plasma membrane (PM) sterol transport in OSH deletion mutants lacking one, several, or all Osh proteins. In conditional OSH mutants, ER-PM ergosterol transport slowed ~20-fold compared with cells expressing a full complement of Osh proteins. Although this initial finding suggested that Osh proteins act as sterol LTPs, the situation is far more complex. Osh proteins have established roles in Rho small GTPase signaling. Osh proteins reinforce cell polarization and they specifically affect the localization of proteins involved in polarized cell growth such as septins, and the GTPases Cdc42p, Rho1p, and Sec4p. In addition, Osh proteins are required for a specific pathway of polarized secretion to sites of membrane growth, suggesting that this is how Osh proteins affect Cdc42p- and Rho1p-dependent polarization. Our findings suggest that Osh proteins integrate sterol trafficking and sterol-dependent cell signaling with the control of cell polarization. |
| doi_str_mv | 10.1007/s11010-008-9999-7 |
| format | Article |
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These properties make ORPs attractive candidates for lipid transfer proteins (LTPs) that directly mediate nonvesicular sterol transfer to the plasma membrane. To test whether yeast ORPs (the Osh proteins) are sterol LTPs, we studied endoplasmic reticulum (ER)-to-plasma membrane (PM) sterol transport in OSH deletion mutants lacking one, several, or all Osh proteins. In conditional OSH mutants, ER-PM ergosterol transport slowed ~20-fold compared with cells expressing a full complement of Osh proteins. Although this initial finding suggested that Osh proteins act as sterol LTPs, the situation is far more complex. Osh proteins have established roles in Rho small GTPase signaling. Osh proteins reinforce cell polarization and they specifically affect the localization of proteins involved in polarized cell growth such as septins, and the GTPases Cdc42p, Rho1p, and Sec4p. In addition, Osh proteins are required for a specific pathway of polarized secretion to sites of membrane growth, suggesting that this is how Osh proteins affect Cdc42p- and Rho1p-dependent polarization. Our findings suggest that Osh proteins integrate sterol trafficking and sterol-dependent cell signaling with the control of cell polarization.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/s11010-008-9999-7</identifier><identifier>PMID: 19125315</identifier><language>eng</language><publisher>Boston: Boston : Springer US</publisher><subject>Biochemistry ; Biomedical and Life Sciences ; Cardiology ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; Cell Polarity ; Cellular biology ; Cholesterol ; Endoplasmic Reticulum - metabolism ; Enzymes ; Life Sciences ; Medical Biochemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Oncology ; Polarization ; Protein Transport ; Proteins ; Receptors, Steroid - genetics ; Receptors, Steroid - metabolism ; rho GTP-Binding Proteins - metabolism ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Sterols - metabolism ; Yeast ; Yeasts</subject><ispartof>Molecular and cellular biochemistry, 2009-06, Vol.326 (1-2), p.9-13</ispartof><rights>Springer Science+Business Media, LLC. 2008</rights><rights>Springer Science+Business Media, LLC. 2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c424t-1ff27341c5c9c526b96a111510fa60c20a644d60c31aa9de035b3dacae5803de3</citedby><cites>FETCH-LOGICAL-c424t-1ff27341c5c9c526b96a111510fa60c20a644d60c31aa9de035b3dacae5803de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11010-008-9999-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11010-008-9999-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19125315$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Beh, Christopher T</creatorcontrib><creatorcontrib>Alfaro, Gabriel</creatorcontrib><creatorcontrib>Duamel, Giselle</creatorcontrib><creatorcontrib>Sullivan, David P</creatorcontrib><creatorcontrib>Kersting, Michael C</creatorcontrib><creatorcontrib>Dighe, Shubha</creatorcontrib><creatorcontrib>Kozminski, Keith G</creatorcontrib><creatorcontrib>Menon, Anant K</creatorcontrib><title>Yeast oxysterol-binding proteins: sterol transporters or regulators of cell polarization?</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) are a conserved family of soluble cytoplasmic proteins that can bind sterols, translocate between membrane compartments, and affect sterol trafficking. 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In addition, Osh proteins are required for a specific pathway of polarized secretion to sites of membrane growth, suggesting that this is how Osh proteins affect Cdc42p- and Rho1p-dependent polarization. Our findings suggest that Osh proteins integrate sterol trafficking and sterol-dependent cell signaling with the control of cell polarization.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cardiology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Polarity</subject><subject>Cellular biology</subject><subject>Cholesterol</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Enzymes</subject><subject>Life Sciences</subject><subject>Medical Biochemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Oncology</subject><subject>Polarization</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Receptors, Steroid - genetics</subject><subject>Receptors, Steroid - metabolism</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - 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| subjects | Biochemistry Biomedical and Life Sciences Cardiology Carrier Proteins - metabolism Cell Membrane - metabolism Cell Polarity Cellular biology Cholesterol Endoplasmic Reticulum - metabolism Enzymes Life Sciences Medical Biochemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Oncology Polarization Protein Transport Proteins Receptors, Steroid - genetics Receptors, Steroid - metabolism rho GTP-Binding Proteins - metabolism Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sterols - metabolism Yeast Yeasts |
| title | Yeast oxysterol-binding proteins: sterol transporters or regulators of cell polarization? |
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