scholarly journals Membrane localization of paralogous leucine permeases Bap2 and Bap3 is regulated by Bul1

2020 ◽  
Author(s):  
S. Maheswaran ◽  
Paike Jayadeva Bhat
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcriptional Regulation ◽  
Plasma Membrane ◽  
Growth Retardation ◽  
Membrane Localization ◽  
Leucine Uptake ◽  
Synthetically Lethal ◽  
Severe Growth

AbstractTimeliness in expression and degradation of the nutrient permeases is crucial for any organism. In Saccharomyces cerevisiae while transcriptional regulation of permeases has been studied in great detail, post translational events such as trafficking and turnover are poorly understood. We found loss of a leucine permease BAP2, but not other permeases lead to severe growth retardation in presence of glucose or galactose but not in medium containing glycerol and lactate. Leucine prototrophy suppressed the growth retardation, showing BAP2 and LEU2 are synthetically lethal. We discovered that loss of BUL1, an arrestin involved in trafficking of diverse permeases suppressed this lethality. The suppression was dependent on another leucine permease, BAP3. Further experiments revealed that in bul1Δ cells, both BAP2 and BAP3 accumulated in plasma membrane and their turnover is reduced. Based on our results and what is known, we propose that BUL1 regulates TORC1 activity by controlling the leucine uptake.

scholarly journals Palmitoylation and Plasma Membrane Localization of Ras2p by a Nonclassical Trafficking Pathway in Saccharomyces cerevisiae

2003 ◽  
Vol 23 (18) ◽  
pp. 6574-6584 ◽  
Author(s):  
Xiangwen Dong ◽  
David A. Mitchell ◽  
Sandra Lobo ◽  
Lihong Zhao ◽  
Douglas J. Bartels ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Secretory Pathway ◽  
Brefeldin A ◽  
Covalent Attachment ◽  
Membrane Localization ◽  
Ras Proteins ◽  
Plasma Membrane Localization ◽  
Additional Processing ◽  
Endomembrane Trafficking

ABSTRACT Subcellular localization of Ras proteins to the plasma membrane is accomplished in part by covalent attachment of a farnesyl moiety to the conserved CaaX box cysteine. Farnesylation targets Ras to the endoplasmic reticulum (ER), where additional processing steps occur, resulting in translocation of Ras to the plasma membrane. The mechanism(s) by which this occurs is not well understood. In this report, we show that plasma membrane localization of Ras2p in Saccharomyces cerevisiae does not require the classical secretory pathway or a functional Golgi apparatus. However, when the classical secretory pathway is disrupted, plasma membrane localization requires Erf2p, a protein that resides in the ER membrane and is required for efficient palmitoylation of Ras2p. Deletion of ERF2 results in a Ras2p steady-state localization defect that is more severe when combined with sec-ts mutants or brefeldin A treatment. The Erf2p-dependent localization of Ras2p correlates with the palmitoylation of Cys-318. An Erf2p-Erf4p complex has recently been shown to be an ER-associated palmitoyltransferase that can palmitoylate Cys-318 of Ras2p (S. Lobo, W. K. Greentree, M. E. Linder, and R. J. Deschenes, J. Biol. Chem. 277:41268-41273, 2002). Erf2-dependent palmitoylation as well as localization of Ras2p requires a region of the hypervariable domain adjacent to the CaaX box. These results provide evidence for the existence of a palmitoylation-dependent, nonclassical endomembrane trafficking system for the plasma membrane localization of Ras proteins.

scholarly journals Functional expression, quantification and cellular localization of the Hxt2 hexose transporter of Saccharomyces cerevisiae tagged with the green fluorescent protein

1999 ◽  
Vol 339 (2) ◽  
pp. 299-307 ◽  
Author(s):  
Arthur L. KRUCKEBERG ◽  
Ling YE ◽  
Jan A. BERDEN ◽  
Karel van DAM
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Green Fluorescent Protein ◽  
Glucose Transport ◽  
Cellular Localization ◽  
Fluorescent Protein ◽  
Hexose Transporter ◽  
High Concentrations ◽  
Green Fluorescent

The Hxt2 glucose transport protein of Saccharomyces cerevisiae was genetically fused at its C-terminus with the green fluorescent protein (GFP). The Hxt2-GFP fusion protein is a functional hexose transporter: it restored growth on glucose to a strain bearing null mutations in the hexose transporter genes GAL2 and HXT1 to HXT7. Furthermore, its glucose transport activity in this null strain was not markedly different from that of the wild-type Hxt2 protein. We calculated from the fluorescence level and transport kinetics that induced cells had 1.4×105 Hxt2-GFP molecules per cell, and that the catalytic-centre activity of the Hxt2-GFP molecule in vivo is 53 s-1 at 30 °C. Expression of Hxt2-GFP was induced by growth at low concentrations of glucose. Under inducing conditions the Hxt2-GFP fluorescence was localized to the plasma membrane. In a strain impaired in the fusion of secretory vesicles with the plasma membrane, the fluorescence accumulated in the cytoplasm. When induced cells were treated with high concentrations of glucose, the fluorescence was redistributed to the vacuole within 4 h. When endocytosis was genetically blocked, the fluorescence remained in the plasma membrane after treatment with high concentrations of glucose.

scholarly journals High yield expression of the Neurospora crassa plasma membrane H(+)-ATPase in Saccharomyces cerevisiae

1994 ◽  
Vol 269 (26) ◽  
pp. 17705-17712
Author(s):  
S.K. Mahanty ◽  
U.S. Rao ◽  
R.A. Nicholas ◽  
G.A. Scarborough
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Neurospora Crassa ◽  
High Yield

scholarly journals Lipid binding by the N-terminal motif mediates plasma membrane localization of Bordetella effector protein BteA

2021 ◽  
pp. 100607
Author(s):  
Ivana Malcova ◽  
Ladislav Bumba ◽  
Filip Uljanic ◽  
Darya Kuzmenko ◽  
Jana Nedomova ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Binding ◽  
Membrane Localization ◽  
Effector Protein ◽  
Plasma Membrane Localization
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