JBC Oz Biosciences

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 Na, S.
Right arrow Articles by Haber, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Na, S.
Right arrow Articles by Haber, J. E.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 270, Number 12, Issue of March 24, 1995 pp. 6815-6823
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
MOP2 (SLA2) Affects the Abundance of the Plasma Membrane H-ATPase of Saccharomyces cerevisiae(*)

(Received for publication, September 27, 1994; and in revised form, January 4, 1995)

Songqing Na(§)(¶) Marina Hincapie(¶)(**) John H. McCusker (§§) James E. Haber (¶¶)

From the Rosenstiel Basic Medical Sciences Research Center and the Department of Biology, Brandeis University, Waltham, Massachusetts 02254


ABSTRACT

The abundance of yeast plasma membrane H-ATPase on the cell surface is tightly regulated. Modifier of pma1 (mop) mutants were isolated as enhancers of the mutant phenotypes of pma1 mutants. mop2 mutations reduce the abundance and activity of Pma1 protein on the plasma membrane without affecting the abundance of other prominent plasma membrane proteins. The MOP2 gene encodes a 108-kDa protein that has previously been identified both as a gene affecting the yeast cytoskeleton (SLA2) (Holtzman, D.A., Yang, S., and Drubin, D. G.(1993) J. Cell Biol. 122, 635-644) and as a gene affecting endocytosis (END4) (Raths, S., Roher, J., Crausaz, F., and Riezman, H.(1993) J. Cell Biol. 120, 55-65). In some strains, MOP2 (SLA2) is essential for cell viability; in others, a deletion mutant is temperature sensitive for growth. mop2 mutations do not reduce the transcription of PMA1 nor do they lead to the accumulation of Pma1 protein in any intracellular compartment. An epitope-tagged MOP2 protein behaves as a plasma membrane-associated protein whose abundance is proportional to its level of gene expression. Over-expression of MOP2 relieved the toxicity caused by the over-expression of PMA1 from a high copy plasmid; conversely, the growth of mop2 strains was inhibited by the presence of a single extra copy of PMA1. We conclude that MOP2 (SLA2) encodes a plasma membrane-associated protein that is required for the accumulation and/or maintenance of plasma membrane H-ATPase on the cell surface.


FOOTNOTES

*
This work was supported by National Institutes of Health Grant GM39739 (to J. E. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked ``advertisement'' in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§
Current address: Pfeizer Corp., Groton, CT 06340.

A major contributor to this paper.

**
A National Institutes of Health Macromolecular Structure and Mechanism pre-doctoral trainee (Training Grant GM07596).

§§
Current address: Dept. of Biochemistry, Stanford University, Stanford, CA 94305.

¶¶
To whom correspondence should be addressed. Tel.: 617-736-2462; Fax: 617-736-2405; haber{at}hydra.rose.brandeis.edu.

(^1)
H. Riezman, personal communication.

(^2)
The abbreviations used are: kb, kilobase(s); PAGE, polyacrylamide gel electrophoresis.

(^3)
H. Riezman, personal communication.


ACKNOWLEDGEMENTS

We thank Sandra Harris for many yeast strains, providing c-Myc monoclonal antibody 9E10, and many suggestions for the experiments, John Teem for providing a monoclonal anti-H-ATPase antibody, and Ed Louis for providing a chromosome separating blot. Xiaochun Zhu carried out the measurements of the effect of mop2 on Pma1 activity. We also thank David Elliott for instructions and suggestions for the immunofluorescence experiments. Discussions with both Howard Reizman and David Drubin are gratefully acknowledged.

Note Added in Proof-Recently, we have found that under some physiological conditions, overexpression of PMA1 can suppress the temperature sensitivity of mop2-2 (M. Hincapie and J. E. Haber, unpublished results).


©1995 by The American Society for Biochemistry and Molecular Biology, Inc.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
GeneticsHome page
S. Yoshiuchi, T. Yamamoto, H. Sakane, J. Kadota, J. Mochida, M. Asaka, and K. Tanaka
Identification of Novel Mutations in ACT1 and SLA2 That Suppress the Actin-Cable-Overproducing Phenotype Caused by Overexpression of a Dominant Active Form of Bni1p in Saccharomyces cerevisiae
Genetics, June 1, 2006; 173(2): 527 - 539.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
G. Ren, P. Vajjhala, J. S. Lee, B. Winsor, and A. L. Munn
The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy
Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 37 - 120.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
J. J. Baggett, K. E. D'Aquino, and B. Wendland
The Sla2p Talin Domain Plays a Role in Endocytosis in Saccharomyces cerevisiae
Genetics, December 1, 2003; 165(4): 1661 - 1674.
[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
FASEB J.Home page
A. V. HUBBERSTEY and E. P. MOTTILLO
Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization
FASEB J, April 1, 2002; 16(6): 487 - 499.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
C. Gatto, S. M. McLoud, and J. H. Kaplan
Heterologous expression of Na+-K+-ATPase in insect cells: intracellular distribution of pump subunits
Am J Physiol Cell Physiol, September 1, 2001; 281(3): C982 - C992.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
S. Waelter, E. Scherzinger, R. Hasenbank, E. Nordhoff, R. Lurz, H. Goehler, C. Gauss, K. Sathasivam, G. P. Bates, H. Lehrach, et al.
The huntingtin interacting protein HIP1 is a clathrin and {alpha}-adaptin-binding protein involved in receptor-mediated endocytosis
Hum. Mol. Genet., August 1, 2001; 10(17): 1807 - 1817.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
C. M. Asleson, E. S. Bensen, C. A. Gale, A.-S. Melms, C. Kurischko, and J. Berman
Candida albicans INT1-Induced Filamentation in Saccharomyces cerevisiae Depends on Sla2p
Mol. Cell. Biol., February 15, 2001; 21(4): 1272 - 1284.
[Abstract] [Full Text]


Home page
JCBHome page
A. E.Y. Engqvist-Goldstein, M. M. Kessels, V. S. Chopra, M. R. Hayden, and D. G. Drubin
An Actin-binding Protein of the Sla2/Huntingtin Interacting Protein 1 Family Is a Novel Component of Clathrin-coated Pits and Vesicles
J. Cell Biol., December 27, 1999; 147(7): 1503 - 1518.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
D. Zuk, J. P. Belk, and A. Jacobson
Temperature-Sensitive Mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 Genes Result in Defects in mRNA Turnover
Genetics, September 1, 1999; 153(1): 35 - 47.
[Abstract] [Full Text]


Home page
Mol. Biol. CellHome page
S. Yang, M. J. T. V. Cope, and D. G. Drubin
Sla2p Is Associated with the Yeast Cortical Actin Cytoskeleton via Redundant Localization Signals
Mol. Biol. Cell, July 1, 1999; 10(7): 2265 - 2283.
[Abstract] [Full Text]


Home page
JCBHome page
M.J. T.V. Cope, S. Yang, C. Shang, and D. G. Drubin
Novel Protein Kinases Ark1p and Prk1p Associate with and Regulate the Cortical Actin Cytoskeleton in Budding Yeast
J. Cell Biol., March 22, 1999; 144(6): 1203 - 1218.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
A. M. Maldonado, N. de la Fuente, and F. Portillo
Characterization of an Allele-Nonspecific Intragenic Suppressor in the Yeast Plasma Membrane H+-ATPase Gene (PMA1)
Genetics, September 1, 1998; 150(1): 11 - 19.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
N. D. DeWitt, C. F. T. dos Santos, K. E. Allen, and C. W. Slayman
Phosphorylation Region of the Yeast Plasma-membrane H+-ATPase. ROLE IN PROTEIN FOLDING AND BIOGENESIS
J. Biol. Chem., August 21, 1998; 273(34): 21744 - 21751.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Kaouass, I. Gamache, D. Ramotar, M. Audette, and R. Poulin
The Spermidine Transport System Is Regulated by Ligand Inactivation, Endocytosis, and by the Npr1p Ser/Thr Protein Kinase in Saccharomyces cerevisiae
J. Biol. Chem., January 23, 1998; 273(4): 2109 - 2117.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
A. Wesp, L. Hicke, J. Palecek, R. Lombardi, T. Aust, A.L. Munn, and H. Riezman
End4p/Sla2p Interacts with Actin-associated Proteins for Endocytosis in Saccharomyces cerevisiae
Mol. Biol. Cell, November 1, 1997; 8(11): 2291 - 2306.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
E. J. Bowman, F. J. O'Neill, and B. J. Bowman
Mutations of pma-1, the Gene Encoding the Plasma Membrane H+-ATPase of Neurospora crassa, Suppress Inhibition of Growth by Concanamycin A, a Specific Inhibitor of Vacuolar ATPases
J. Biol. Chem., June 6, 1997; 272(23): 14776 - 14786.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
R. O. McCann and S. W. Craig
The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
PNAS, May 27, 1997; 94(11): 5679 - 5684.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. S. Hackam, A. S. Yassa, R. Singaraja, M. Metzler, C.-A. Gutekunst, L. Gan, S. Warby, C. L. Wellington, J. Vaillancourt, N. Chen, et al.
Huntingtin Interacting Protein 1 Induces Apoptosis via a Novel Caspase-dependent Death Effector Domain
J. Biol. Chem., December 22, 2000; 275(52): 41299 - 41308.
[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 © 1995 by the American Society for Biochemistry and Molecular Biology.