Ubiquitination and Endocytosis of Plasma Membrane Proteins: Role of Nedd4/Rsp5p Family of Ubiquitin-Protein Ligases

2000 ◽  
Vol 176 (1) ◽  
pp. 1-17 ◽  
Author(s):  
D. Rotin ◽  
O. Staub ◽  
R. Haguenauer-Tsapis
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plasma Membrane Proteins ◽  
Protein Ligases

Granules and vesicles of human neutrophils. The role of endomembranes as source of plasma membrane proteins

2009 ◽  
Vol 51 (5) ◽  
pp. 318-322 ◽  
Author(s):  
Niels Borregaard ◽  
Lars Kjeldsen ◽  
Karsten Lollike ◽  
Henrik Sengeløv
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Human Neutrophils ◽  
Plasma Membrane Proteins

scholarly journals Phosphatidylserine translocation at the yeasttrans-Golgi network regulates protein sorting into exocytic vesicles

2015 ◽  
Vol 26 (25) ◽  
pp. 4674-4685 ◽  
Author(s):  
Hannah M. Hankins ◽  
Yves Y. Sere ◽  
Nicholas S. Diab ◽  
Anant K. Menon ◽  
Todd R. Graham
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Primary Role ◽  
Plasma Membrane Proteins ◽  
Critical Function ◽  
Oxysterol Binding Protein ◽  
Phosphatidylserine Translocation ◽  
Golgi Network ◽  
Lateral Segregation

Sorting of plasma membrane proteins into exocytic vesicles at the yeast trans-Golgi network (TGN) is believed to be mediated by their coalescence with specific lipids, but how these membrane-remodeling events are regulated is poorly understood. Here we show that the ATP-dependent phospholipid flippase Drs2 is required for efficient segregation of cargo into exocytic vesicles. The plasma membrane proteins Pma1 and Can1 are missorted from the TGN to the vacuole in drs2∆ cells. We also used a combination of flippase mutants that either gain or lose the ability to flip phosphatidylserine (PS) to determine that PS flip by Drs2 is its critical function in this sorting event. The primary role of PS flip at the TGN appears to be to control the oxysterol-binding protein homologue Kes1/Osh4 and regulate ergosterol subcellular distribution. Deletion of KES1 suppresses plasma membrane–missorting defects and the accumulation of intracellular ergosterol in drs2 mutants. We propose that PS flip is part of a homeostatic mechanism that controls sterol loading and lateral segregation of protein and lipid domains at the TGN.

scholarly journals A specific role of AGS3 in the surface expression of plasma membrane proteins

2007 ◽  
Vol 104 (46) ◽  
pp. 18103-18108 ◽  
Author(s):  
B. Groves ◽  
Q. Gong ◽  
Z. Xu ◽  
C. Huntsman ◽  
C. Nguyen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Surface Expression ◽  
Specific Role ◽  
Plasma Membrane Proteins

The Role of Plasma Membrane Proteins in Tolerance of Dehydration in the Plant Cell

2019 ◽  
pp. 339-348
Author(s):  
Pragya Barua ◽  
Dipak Gayen ◽  
Nilesh Vikram Land ◽  
Subhra Chakraborty ◽  
Niranjan Chakraborty
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plant Cell ◽  
Plasma Membrane Proteins

scholarly journals Deubiquitination Step in the Endocytic Pathway of Yeast Plasma Membrane Proteins: Crucial Role of Doa4p Ubiquitin Isopeptidase

2001 ◽  
Vol 21 (14) ◽  
pp. 4482-4494 ◽  
Author(s):  
S. Dupré ◽  
R. Haguenauer-Tsapis
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Degradation Products ◽  
Endocytic Pathway ◽  
Plasma Membrane Proteins ◽  
General Role ◽  
Yeast Plasma Membrane ◽  
Membrane Bound ◽  
Vacuolar Protein

ABSTRACT The Fur4p uracil permease, like most yeast plasma membrane proteins, undergoes ubiquitin-dependent endocytosis and is then targeted to the vacuole (equivalent to the mammalian lysosome) for degradation. The cell surface ubiquitination of Fur4p is mediated by the essential Rsp5p ubiquitin ligase. Ubiquitination of Fur4p occurs on two target lysines, which receive two ubiquitin moieties linked through ubiquitin Lys63, a type of linkage (termed UbK63) different from that involved in proteasome recognition. We report that pep4cells deficient for vacuolar protease activities accumulate vacuolar unubiquitinated Fur4p. In contrast, pep4 cells lacking the Doa4p ubiquitin isopeptidase accumulate ubiquitin-conjugated Fur4p. These data suggest that Fur4p undergoes Doa4p-dependent deubiquitination prior to vacuolar degradation. Compared topep4 cells, pep4 doa4 cells have huge amounts of membrane-bound ubiquitin conjugates. This indicates that Doa4p plays a general role in the deubiquitination of membrane-bound proteins, as suggested by reports describing the suppression of somedoa4 phenotypes in endocytosis and vacuolar protein sorting mutants. Some of the small ubiquitin-linked peptides that are a hallmark of Doa4 deficiency are not present in rsp5 mutant cells or after overproduction of a variant ubiquitin modified at Lys 63 (UbK63R). These data suggest that the corresponding peptides are degradation products of Rsp5p substrates and probably of ubiquitin conjugates carrying UbK63 linkages. Doa4p thus appears to be involved in the deubiquitination of endocytosed plasma membrane proteins, some of them carrying UbK63 linkages.

Detergent fractionation with subsequent subtractive suppression hybridization as a tool for identifying genes coding for plasma membrane proteins

2009 ◽  
Vol 18 (6) ◽  
pp. 527-535 ◽  
Author(s):  
Andreas Lange ◽  
Claudia Kistler ◽  
Tanja B. Jutzi ◽  
Alexandr V. Bazhin ◽  
Claus Detlev Klemke ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plasma Membrane Proteins ◽  
Subtractive Suppression Hybridization

scholarly journals pH-dependent Cargo Sorting from the Golgi

2011 ◽  
Vol 286 (12) ◽  
pp. 10058-10065 ◽  
Author(s):  
Chunjuan Huang ◽  
Amy Chang
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Atpase Activity ◽  
Secretory Pathway ◽  
Ph Dependence ◽  
Glucose Deprivation ◽  
Ph Homeostasis ◽  
Plasma Membrane Proteins ◽  
Cytosolic Ph ◽  
Cargo Sorting

The vacuolar proton-translocating ATPase (V-ATPase) plays a major role in organelle acidification and works together with other ion transporters to maintain pH homeostasis in eukaryotic cells. We analyzed a requirement for V-ATPase activity in protein trafficking in the yeast secretory pathway. Deficiency of V-ATPase activity caused by subunit deletion or glucose deprivation results in missorting of newly synthesized plasma membrane proteins Pma1 and Can1 directly from the Golgi to the vacuole. Vacuolar mislocalization of Pma1 is dependent on Gga adaptors although no Pma1 ubiquitination was detected. Proper cell surface targeting of Pma1 was rescued in V-ATPase-deficient cells by increasing the pH of the medium, suggesting that missorting is the result of aberrant cytosolic pH. In addition to mislocalization of the plasma membrane proteins, Golgi membrane proteins Kex2 and Vrg4 are also missorted to the vacuole upon loss of V-ATPase activity. Because the missorted cargos have distinct trafficking routes, we suggest a pH dependence for multiple cargo sorting events at the Golgi.

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