A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway

Harsay, Edina; Schekman, Randy

doi:10.1083/jcb.200109077

Cited by 132 publications

(158 citation statements)

References 84 publications

(129 reference statements)

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“…In this mutant, postGolgi secretory vesicles accumulate in the cytoplasm at the restrictive temperature. It has been shown that yeast cells have at least two types of secretory vesicles that are delivered to the plasma membrane for exocytosis (Harsay and Bretscher 1995;Harsay and Schekman 2002). The invertase vesicles carry proteins such as invertase, acid phosphatase, and possibly the general amino acid permease (Roberg et al 1997), which are secreted only under certain specific physiological conditions.…”

Section: The Rho Family Of Small Gtp-binding Proteinsmentioning

confidence: 99%

Membrane Organization and Dynamics in Cell Polarity

Orlando¹,

Guo²

2009

Cold Spring Harbor Perspectives in Biology

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The establishment and maintenance of cell polarity is important to a wide range of biological processes ranging from chemotaxis to embryogenesis. An essential feature of cell polarity is the asymmetric organization of proteins and lipids in the plasma membrane. In this article, we discuss how polarity regulators such as small GTP-binding proteins and phospholipids spatially and kinetically control vesicular trafficking and membrane organization. Conversely, we discuss how membrane trafficking contributes to cell polarization through delivery of polarity determinants and regulators to the plasma membrane.

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Section: The Rho Family Of Small Gtp-binding Proteinsmentioning

confidence: 99%

Membrane Organization and Dynamics in Cell Polarity

Orlando¹,

Guo²

2009

Cold Spring Harbor Perspectives in Biology

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“…From the Golgi complex, Pma1 is transported to the cell surface by a branch of the secretory pathway that does not intersect with endosomes [7,8]. At the cell surface, Pma1 becomes stabilized by a poorly characterized mechanism and occupies detergent-resistant domains that are distinct from those occupied by the arginine/H þ symporter Can1 [9,10].…”

Section: Biogenesis and Transport Of The Proton Pumping H D -Atpasementioning

confidence: 99%

“…In wild-type cells these two vesicle populations have different densities. The high-density vesicles contain invertase and acid phosphatase and intersect with the endosomal system, whereas the low-density vesicles contain Pma1 and glucanase and are directly transported to the cell surface without intersection with endosomes [7]. Elongase mutants on the other hand fail to generate these two vesicle populations and instead missort invertase and acid phosphatase into the Pma1 containing vesicle [30].…”

Section: Coupling Of H D -Atpase Biogenesis To Sphingolipid Synthesismentioning

confidence: 99%

Lipid-dependent surface transport of the proton pumping ATPase: A model to study plasma membrane biogenesis in yeast

Toulmay

Schneiter

2007

Biochimie

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The proton pumping H þ -ATPase, Pma1, is one of the most abundant integral membrane proteins of the yeast plasma membrane. Pma1 activity controls the intracellular pH and maintains the electrochemical gradient across the plasma membrane, two essential cellular functions. The maintenance of the proton gradient, on the other hand, also requires a specialized lipid composition of this membrane. The plasma membrane of eukaryotic cells is typically rich in sphingolipids and sterols. These two lipids condense to form less fluid membrane microdomains or lipid rafts. The yeast sphingolipid is peculiar in that it invariably contains a saturated very long-chain fatty acid with 26 carbon atoms. During cell growth and plasma membrane expansion, both C26-containing sphingolipids and Pma1 are first synthesized in the endoplasmatic reticulum from where they are transported by the secretory pathway to the cell surface. Remarkably, shortening the C26 fatty acid to a C22 fatty acid by mutations in the fatty acid elongation complex impairs raft association of newly synthesized Pma1 and induces rapid degradation of the ATPase by rerouting the enzyme from the plasma membrane to the vacuole, the fungal equivalent of the lysosome. Here, we review the role of lipids in mediating raft association and stable surface transport of the newly synthesized ATPase, and discuss a model, in which the newly synthesized ATPase assembles into a membrane environment that is enriched in C26-containing lipids already in the endoplasmatic reticulum. The resulting proteinelipid complex is then transported and sorted as an entity to the plasma membrane. Failure to successfully assemble this lipideprotein complex results in mistargeting of the protein to the vacuole.

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“…This complex is then packaged into a larger subclass of COPII transport vesicles that contain Lst1p in addition to Sec24p (3) and is transported to the cell surface by a branch of the secretory pathway that does not intersect with endosomes (4,5). Once at surface, Pma1p becomes stabilized and occupies domains that are distinct from those occupied by the arginine/H ϩ symporter Can1p (6).…”

mentioning

confidence: 99%

Very Long-chain Fatty Acid-containing Lipids rather than Sphingolipids per se Are Required for Raft Association and Stable Surface Transport of Newly Synthesized Plasma Membrane ATPase in Yeast

Gaigg

Toulmay

Schneiter

2006

Journal of Biological Chemistry

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The proton-pumping H ؉ -ATPase, Pma1p, is an abundant and very long lived polytopic protein of the yeast plasma membrane. Pma1p constitutes a major cargo of the secretory pathway and thus serves as a model to study plasma membrane biogenesis. Pma1p associates with detergent-resistant membrane domains (lipid "rafts") already in the ER, and a lack of raft association correlates with mistargeting of the protein to the vacuole, where it is degraded. We are analyzing the role of specific lipids in membrane domain formation and have previously shown that surface transport of Pma1p is independent of newly synthesized sterols but that sphingolipids with C26 very long chain fatty acid are crucial for raft association and surface transport of Pma1p (Gaigg, B., Timischl, B., Corbino, L., and Schneiter, R. (2005) J. Biol. Chem. 280, 22515-22522). We now describe a more detailed analysis of the function that sphingolipids play in this process. Using a yeast strain in which the essential function of sphingolipids is substituted by glycerophospholipids containing C26 very long chain fatty acids, we find that sphingolipids per se are dispensable for raft association and surface delivery of Pma1p but that the C26 fatty acid is crucial. We thus conclude that the essential function of sphingolipids for membrane domain formation and stable surface delivery of Pma1p is provided by the C26 fatty acid that forms part of the yeast ceramide.

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A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway

Cited by 132 publications

References 84 publications

Membrane Organization and Dynamics in Cell Polarity

Membrane Organization and Dynamics in Cell Polarity

Lipid-dependent surface transport of the proton pumping ATPase: A model to study plasma membrane biogenesis in yeast

Very Long-chain Fatty Acid-containing Lipids rather than Sphingolipids per se Are Required for Raft Association and Stable Surface Transport of Newly Synthesized Plasma Membrane ATPase in Yeast

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