JBC Invitrogen Ultrasensitive Cytokine Assays

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by DeWitt, N. D.
Right arrow Articles by Slayman, C. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by DeWitt, N. D.
Right arrow Articles by Slayman, C. W.

J Biol Chem, Vol. 273, Issue 34, 21744-21751, August 21, 1998

Phosphorylation Region of the Yeast Plasma-membrane H+-ATPase
ROLE IN PROTEIN FOLDING AND BIOGENESIS

Natalie D. DeWitt, Carlos F. Tourinho dos Santos, Kenneth E. Allen, and Carolyn W. Slayman

From the Departments of Genetics and Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510

Mutations at the phosphorylation site (Asp-378) of the yeast plasma-membrane H+-ATPase have been shown previously to cause misfolding of the ATPase, preventing normal movement along the secretory pathway; Asp-378 mutations also block the biogenesis of co-expressed wild-type ATPase and lead to a dominant lethal phenotype. To ask whether these defects are specific for Asp-378 or whether the phosphorylation region as a whole is involved, alanine-scanning mutagenesis has been carried out to examine the role of 11 conserved residues flanking Asp-378. In the sec6-4 expression system (Nakamoto, R. K., Rao, R., and Slayman, C. W. (1991) J. Biol. Chem. 266, 7940-7949), the mutant ATPases displayed varying abilities to reach the secretory vesicles that deliver plasma-membrane proteins to the cell surface. Indirect immunofluorescence of intact cells also gave evidence for a spectrum of behavior, ranging from mutant ATPases completely arrested (D378A, K379A, T380A, and T384A) or partially arrested in the endoplasmic reticulum to those that reached the plasma membrane in normal amounts (C376A, S377A, and G381A). Although the extent of ER retention varied among the mutants, the endoplasmic reticulum appeared to be the only secretory compartment in which the mutant ATPases accumulated. All of the mutant proteins that localized either partially or fully to the ER were also malfolded based on their abnormal sensitivity to trypsin. Among them, the severely affected mutants had a dominant lethal phenotype, and even the intermediate mutants caused a visible slowing of growth when co-expressed with wild-type ATPase. The effects on growth could be traced to the trapping of the wild-type enzyme with the mutant enzyme in the ER, as visualized by double label immunofluorescence. Taken together, the results indicate that the residues surrounding Asp-378 are critically important for ATPase maturation and transport to the cell surface.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
L. Pineau, L. Bonifait, J.-M. Berjeaud, P. Alimardani-Theuil, T. Berges, and T. Ferreira
A Lipid-mediated Quality Control Process in the Golgi Apparatus in Yeast
Mol. Biol. Cell, March 1, 2008; 19(3): 807 - 821.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Han, Y. Liu, and A. Chang
Cytoplasmic Hsp70 Promotes Ubiquitination for Endoplasmic Reticulum-associated Degradation of a Misfolded Mutant of the Yeast Plasma Membrane ATPase, PMA1
J. Biol. Chem., September 7, 2007; 282(36): 26140 - 26149.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. B. Mason, K. E. Allen, and C. W. Slayman
Effects of C-terminal Truncations on Trafficking of the Yeast Plasma Membrane H+-ATPase
J. Biol. Chem., August 18, 2006; 281(33): 23887 - 23898.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
Y. Liu and A. Chang
Quality control of a mutant plasma membrane ATPase: ubiquitylation prevents cell-surface stability
J. Cell Sci., January 15, 2006; 119(2): 360 - 369.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
S. Wicky, H. Schwarz, and B. Singer-Kruger
Molecular Interactions of Yeast Neo1p, an Essential Member of the Drs2 Family of Aminophospholipid Translocases, and Its Role in Membrane Trafficking within the Endomembrane System
Mol. Cell. Biol., September 1, 2004; 24(17): 7402 - 7418.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Q. Wang and A. Chang
Sphingoid base synthesis is required for oligomerization and cell surface stability of the yeast plasma membrane ATPase, Pma1
PNAS, October 1, 2002; 99(20): 12853 - 12858.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Ferreira, A. B. Mason, M. Pypaert, K. E. Allen, and C. W. Slayman
Quality Control in the Yeast Secretory Pathway. A MISFOLDED PMA1 H+-ATPase REVEALS TWO CHECKPOINTS
J. Biol. Chem., May 31, 2002; 277(23): 21027 - 21040.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
X. Gong and A. Chang
A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface
PNAS, July 31, 2001; 98(16): 9104 - 9109.
[Abstract] [Full Text] [PDF]

Home page
 J. Exp. Biol.Home page
A Ambesi, M Miranda, V. Petrov, and C. Slayman
Biogenesis and function of the yeast plasma-membrane H(+)-ATPase
J. Exp. Biol., January 1, 2000; 203(1): 155 - 160.
[Abstract]

Home page
 J. Biol. Chem.Home page
S. S. Gupta, N. D. DeWitt, K. E. Allen, and C. W. Slayman
Evidence for a Salt Bridge between Transmembrane Segments 5 and 6 of the Yeast Plasma-membrane H+-ATPase
J. Biol. Chem., December 18, 1998; 273(51): 34328 - 34334.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Ambesi, M. Miranda, K. E. Allen, and C. W. Slayman
Stalk Segment 4 of the Yeast Plasma Membrane H+-ATPase. MUTATIONAL EVIDENCE FOR A ROLE IN THE E1-E2 CONFORMATIONAL CHANGE
J. Biol. Chem., June 30, 2000; 275(27): 20545 - 20550.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Perzov, H. Nelson, and N. Nelson
Altered Distribution of the Yeast Plasma Membrane H+-ATPase as a Feature of Vacuolar H+-ATPase Null Mutants
J. Biol. Chem., December 15, 2000; 275(51): 40088 - 40095.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Soteropoulos, A. Valiakhmetov, R. Kashiwazaki, and D. S. Perlin
Helical Stalk Segments S4 and S5 of the Plasma Membrane H+-ATPase from Saccharomyces cerevisiae Are Optimized to Impact Catalytic Site Environment
J. Biol. Chem., May 4, 2001; 276(19): 16265 - 16270.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Miranda, K. E. Allen, J. P. Pardo, and C. W. Slayman
Stalk Segment 5 of the Yeast Plasma Membrane H+-ATPase. MUTATIONAL EVIDENCE FOR A ROLE IN GLUCOSE REGULATION
J. Biol. Chem., June 15, 2001; 276(25): 22485 - 22490.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Ferreira, A. B. Mason, and C. W. Slayman
The Yeast Pma1 Proton Pump: a Model for Understanding the Biogenesis of Plasma Membrane Proteins
J. Biol. Chem., August 3, 2001; 276(32): 29613 - 29616.
[Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.