Molecular Biology of the Cell Sign up for new MBC in Press e-TOCs!

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Originally published as MBC in Press, 10.1091/mbc.01-06-0301 on March 7, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
01-06-0301v1
13/5/1626    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Dunand-Sauthier, I.
Right arrow Articles by Humphrey, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dunand-Sauthier, I.
Right arrow Articles by Humphrey, T.

Vol. 13, Issue 5, 1626-1640, May 2002

Sum1, a Component of the Fission Yeast eIF3 Translation Initiation Complex, Is Rapidly Relocalized During Environmental Stress and Interacts with Components of the 26S Proteasome

Isabelle Dunand-Sauthier,* Carol Walker,* Caroline Wilkinson,dagger Colin Gordon,dagger Richard Crane,Dagger Chris Norbury,Dagger and Tim Humphrey*§

 *Cell Cycle Laboratory, Medical Research Council, Radiation and Genome Stability Unit, Harwell, Didcot, OX11 0RD, United Kingdom;  dagger MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh, EH4 2XU, United Kingdom; and  Dagger Imperial Cancer Research Fund, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, OX3 9DS, United Kingdom

Eukaryotic translation initiation factor 3 (eIF3) is a multisubunit complex that plays a central role in translation initiation. We show that fission yeast Sum1, which is structurally related to known eIF3 subunits in other species, is essential for translation initiation, whereas its overexpression results in reduced global translation. Sum1 is associated with the 40S ribosome and interacts stably with Int6, an eIF3 component, in vivo, suggesting that Sum1 is a component of the eIF3 complex. Sum1 is cytoplasmic under normal growth conditions. Surprisingly, Sum1 is rapidly relocalized to cytoplasmic foci after osmotic and thermal stress. Int6 and p116, another putative eIF3 subunit, behave similarly, suggesting that eIF3 is a dynamic complex. These cytoplasmic foci, which additionally comprise eIF4E and RNA components, may function as translation centers during environmental stress. After heat shock, Sum1 additionally colocalizes stably with the 26S proteasome at the nuclear periphery. The relationship between Sum1 and the 26S proteasome was further investigated, and we find cytoplasmic Sum1 localization to be dependent on the 26S proteasome. Furthermore, Sum1 interacts with the Mts2 and Mts4 components of the 26S proteasome. These data indicate a functional link between components of the structurally related eIF3 translation initiation and 26S proteasome complexes.


§ Corresponding author. E-mail address: T.Humphrey{at}har.mrc.ac.uk.


Molecular Biology of the Cell
Vol. 13, 1626-1640, May 2002
Copyright © 2002 by The American Society for Cell Biology



This article has been cited by other articles:


Home page
Eukaryot CellHome page
E. Asp, D. Nilsson, and P. Sunnerhagen
Fission Yeast Mitogen-Activated Protein Kinase Sty1 Interacts with Translation Factors
Eukaryot. Cell, February 1, 2008; 7(2): 328 - 338.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
M. Brengues and R. Parker
Accumulation of Polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-Bodies in Saccharomyces cerevisiae
Mol. Biol. Cell, July 1, 2007; 18(7): 2592 - 2602.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. B. Decca, M. A. Carpio, C. Bosc, M. R. Galiano, D. Job, A. Andrieux, and M. E. Hallak
Post-translational Arginylation of Calreticulin: A NEW ISOSPECIES OF CALRETICULIN COMPONENT OF STRESS GRANULES
J. Biol. Chem., March 16, 2007; 282(11): 8237 - 8245.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
V. Stribinskis and K. S. Ramos
Rpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies
Nucleic Acids Res., February 28, 2007; 35(4): 1301 - 1311.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. K. LeFebvre, N. L. Korneeva, M. Trutschl, U. Cvek, R. D. Duzan, C. A. Bradley, J. W. B. Hershey, and R. E. Rhoads
Translation Initiation Factor eIF4G-1 Binds to eIF3 through the eIF3e Subunit
J. Biol. Chem., August 11, 2006; 281(32): 22917 - 22932.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
P. Anderson and N. Kedersha
RNA granules
J. Cell Biol., March 13, 2006; 172(6): 803 - 808.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
S. Swaminathan, T. Masek, C. Molin, M. Pospisek, and P. Sunnerhagen
Rck2 Is Required for Reprogramming of Ribosomes during Oxidative Stress
Mol. Biol. Cell, March 1, 2006; 17(3): 1472 - 1482.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
I. Dunand-Sauthier, C. A. Walker, J. Narasimhan, A. K. Pearce, R. C. Wek, and T. C. Humphrey
Stress-Activated Protein Kinase Pathway Functions To Support Protein Synthesis and Translational Adaptation in Response to Environmental Stress in Fission Yeast
Eukaryot. Cell, November 1, 2005; 4(11): 1785 - 1793.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
C. C. L. Jenkins, J. Mata, R. F. Crane, B. Thomas, A. Akoulitchev, J. Bahler, and C. J. Norbury
Activation of AP-1-Dependent Transcription by a Truncated Translation Initiation Factor
Eukaryot. Cell, November 1, 2005; 4(11): 1840 - 1850.
[Abstract] [Full Text] [PDF]


Home page
J. Gen. Virol.Home page
L. Ballut, M. Drucker, M. Pugniere, F. Cambon, S. Blanc, F. Roquet, T. Candresse, H.-P. Schmid, P. Nicolas, O. L. Gall, et al.
HcPro, a multifunctional protein encoded by a plant RNA virus, targets the 20S proteasome and affects its enzymic activities
J. Gen. Virol., September 1, 2005; 86(9): 2595 - 2603.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Miyamoto, P. Patel, and J. W. B. Hershey
Changes in Ribosomal Binding Activity of eIF3 Correlate with Increased Translation Rates during Activation of T Lymphocytes
J. Biol. Chem., August 5, 2005; 280(31): 28251 - 28264.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
D. TEIXEIRA, U. SHETH, M. A. VALENCIA-SANCHEZ, M. BRENGUES, and R. PARKER
Processing bodies require RNA for assembly and contain nontranslating mRNAs
RNA, April 1, 2005; 11(4): 371 - 382.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
A. J. Liska, A. Shevchenko, U. Pick, and A. Katz
Enhanced Photosynthesis and Redox Energy Production Contribute to Salinity Tolerance in Dunaliella as Revealed by Homology-Based Proteomics
Plant Physiology, September 1, 2004; 136(1): 2806 - 2817.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
S. R. Kimball, R. L. Horetsky, D. Ron, L. S. Jefferson, and H. P. Harding
Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes
Am J Physiol Cell Physiol, February 1, 2003; 284(2): C273 - C284.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]