Secretory vesicles externalize the major plasma membrane ATPase in yeast.

Holcomb, Cherie L.; Hansen, Wendy F.; Etcheverry, Tina; Schekman, Randy

doi:10.1083/jcb.106.3.641

Cited by 68 publications

(30 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As with other integral membrane proteins destined for the plasma membrane, Pma1 is biosynthetically inserted into the membrane of the ER, from where it is transported by vesicular carriers to its final destination [2,3]. Already in the ER, Pma1 forms a large 1.8-MDa homo-oligomeric complex that resists extraction by detergents [4].…”

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

confidence: 99%

“…Even though LST1 is not essential, cells lacking LST1 are sensitive to low pH because of a reduced flux of Pma1 out of the ER [5]. During transport, Pma1 is not modified by glycosylation or proteolysis, but the protein becomes phosphorylated on multiple serine and threonine residues [2,3]. The significance of these phosphorylations is still unknown, but there is evidence that at least one of these phosphorylations that occurs at or near the plasma membrane is important for glucose-dependent activation of the enzyme [3,6].…”

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

confidence: 99%

See 1 more Smart Citation

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

Toulmay

Schneiter

2007

Biochimie

View full text Add to dashboard Cite

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.

show abstract

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

confidence: 99%

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

confidence: 99%

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

Toulmay

Schneiter

2007

Biochimie

View full text Add to dashboard Cite

show abstract

“…After translation and insertion into the ER membrane, PMA1 is packaged into COPII vesicles (Shimoni et al, 2000), then transported to the PM via the Golgi, because in various secretory mutants, it remains in the Golgi apparatus (sec7) or in the secretory vesicles trafficking between the Golgi and the PM (sec6 and sec1) (Holcomb et al, 1988;Chang and Slayman, 1991). Moreover, data obtained in yeast suggest a relationship between (1) protein oligomerization and/or association with detergent-resistant membranes and (2) the PM targeting and/or stability of the protein (Patton et al, 1992;Bagnat et al, 2000Bagnat et al, , 2001Gong and Chang, 2001;Lee et al, 2002;Luo et al, 2002;Wang and Chang, 2002).…”

Section: Introductionmentioning

confidence: 99%

Targeting of a Nicotiana plumbaginifolia H⁺-ATPase to the Plasma Membrane Is Not by Default and Requires Cytosolic Structural Determinants

et al. 2004

View full text Add to dashboard Cite

The structural determinants involved in the targeting of multitransmembrane-span proteins to the plasma membrane (PM) remain poorly understood. The plasma membrane H þ -ATPase (PMA) from Nicotiana plumbaginifolia, a well-characterized 10 transmembrane-span enzyme, was used as a model to identify structural elements essential for targeting to the PM. When PMA2 and PMA4, representatives of the two main PMA subfamilies, were fused to green fluorescent protein (GFP), the chimeras were shown to be still functional and to be correctly and rapidly targeted to the PM in transgenic tobacco. By contrast, chimeric proteins containing various combinations of PMA transmembrane spanning domains accumulated in the Golgi apparatus and not in the PM and displayed slow traffic properties through the secretory pathway. Individual deletion of three of the four cytosolic domains did not prevent PM targeting, but deletion of the large loop or of its nucleotide binding domain resulted in GFP fluorescence accumulating exclusively in the endoplasmic reticulum. The results show that, at least for this polytopic protein, the PM is not the default pathway and that, in contrast with single-pass membrane proteins, cytosolic structural determinants are required for correct targeting.

show abstract

“…In S. cerevisiae, Pma1p is delivered to the cell surface via the classical endoplasmic reticulum (ER) to the Golgi secretory pathway defined by the SEC genes (15)(16)(17), where specialized proteins ensure the efficient transport of Pma1p through the secretory pathway. For instance, Lst1p (Sec24p homolog) is involved in the export of Pma1p from the ER.…”

mentioning

confidence: 99%

The Plasma Membrane Proton Pump PMA-1 Is Incorporated into Distal Parts of the Hyphae Independently of the Spitzenkörper in Neurospora crassa

2013

View full text Add to dashboard Cite

bMost models for fungal growth have proposed a directional traffic of secretory vesicles to the hyphal apex, where they temporarily aggregate at the Spitzenkörper before they fuse with the plasma membrane (PM). The PM H ؉ -translocating ATPase (PMA-1) is delivered via the classical secretory pathway (endoplasmic reticulum [ER] to Golgi) to the cell surface, where it pumps H ؉ out of the cell, generating a large electrochemical gradient that supplies energy to H ؉ -coupled nutrient uptake systems. To characterize the traffic and delivery of PMA-1 during hyphal elongation, we have analyzed by laser scanning confocal microscopy (LSCM) strains of Neurospora crassa expressing green fluorescent protein (GFP)-tagged versions of the protein. In conidia, PMA-1-GFP was evenly distributed at the PM. During germination and germ tube elongation, PMA-1-GFP was found all around the conidial PM and extended to the germ tube PM, but fluorescence was less intense or almost absent at the tip. Together, the data indicate that the electrochemical gradient driving apical nutrient uptake is generated from early developmental stages. In mature hyphae, PMA-1-GFP localized at the PM at distal regions (>120 m) and in completely developed septa, but not at the tip, indicative of a distinct secretory route independent of the Spitzenkörper occurring behind the apex. One of the main features of filamentous fungi is their apical mode of growth. In filamentous fungi, cell wall growth and exocytosis are linked processes that involve the highly polarized traffic of cell wall-building secretory vesicles to apical areas, where they deliver proteins and lipids. One of the most widely accepted models for fungal growth, the vesicle supply center for fungal morphogenesis, postulates a unidirectional traffic of vesicles to the hyphal apex, where they aggregate temporarily at an apical structure, the Spitzenkörper, prior to fusion with the apical plasma membrane (PM) by the process of exocytosis (1). However, some PM proteins, such as the H ϩ -ATPases, essential for hyphal growth, have been previously predicted to be absent or inactive at the hyphal apex (2-4), suggesting the existence of vesicle delivery routes other than the above and independent of the Spitzenkörper that reach nonapical regions of the hyphal PM. H ϩ -ATPases are involved in pumping protons out of the cell, generating a large electrochemical gradient and supplying energy to H ϩ -coupled nutrient uptake systems (5). This electrochemical gradient has been studied in several fungal species by diverse methods, including vibrating probes, microelectrodes, and pH indicators. The results showed that current normally flows inward at the hyphal apical regions and flows outward at distal areas (3, 4, 6-9).PMA1, the H ϩ -ATPase-encoding gene in Saccharomyces cerevisiae (SCRG_01016 [10]), has a single homolog in Neurospora crassa (NCU01680 [11,12]). In S. cerevisiae, Pma1p is one of the most abundant proteins of the cell surface (25 to 50%), while in N. crassa, it constitutes about 5 to 10% of the...

show abstract

Secretory vesicles externalize the major plasma membrane ATPase in yeast.

Cited by 68 publications

References 44 publications

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

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

Targeting of a Nicotiana plumbaginifolia H⁺-ATPase to the Plasma Membrane Is Not by Default and Requires Cytosolic Structural Determinants

The Plasma Membrane Proton Pump PMA-1 Is Incorporated into Distal Parts of the Hyphae Independently of the Spitzenkörper in Neurospora crassa

Contact Info

Product

Resources

About

Secretory vesicles externalize the major plasma membrane ATPase in yeast.

Cited by 68 publications

References 44 publications

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

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

Targeting of a Nicotiana plumbaginifolia H+-ATPase to the Plasma Membrane Is Not by Default and Requires Cytosolic Structural Determinants

The Plasma Membrane Proton Pump PMA-1 Is Incorporated into Distal Parts of the Hyphae Independently of the Spitzenkörper in Neurospora crassa

Contact Info

Product

Resources

About

Targeting of a Nicotiana plumbaginifolia H⁺-ATPase to the Plasma Membrane Is Not by Default and Requires Cytosolic Structural Determinants