ArticleMolecular biology of the cell2002
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.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 62 citations in OpenAlex.
- Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth.The Plant cell · 2026Article
- Biogenesis of stress granules and their role in the regulation of stress-induced male reproduction disorders.Cell communication and signaling : CCS · 2025Review
- Proteomic composition of eukaryotic and bacterial RNA decay condensates suggests convergent evolution.Current opinion in microbiology · 2024Review
- Stress-induced inhibition of translation independently of eIF2α phosphorylation.Journal of cell science · 2015Article
- The translational factor eIF3f: the ambivalent eIF3 subunit.Cellular and molecular life sciences : CMLS · 2013Review
- A stress-activated, p38 mitogen-activated protein kinase-ATF/CREB pathway regulates posttranscriptional, sequence-dependent decay of target RNAs.Molecular and cellular biology · 2013Article
- Article
- A forward genetic screen identifies eukaryotic translation initiation factor 3, subunit H (eIF3h), as an enhancer of variegation in the mouse.G3 (Bethesda, Md.) · 2012Article
- Carboxy-terminal phosphorylation sites in Cdc25 contribute to enforcement of the DNA damage and replication checkpoints in fission yeast.Current genetics · 2012Article
- The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6.Oncogene · 2011Article
- RNA granules: the good, the bad and the ugly.Cellular signalling · 2011Review
- Cellular stress induces cytoplasmic RNA granules in fission yeast.RNA (New York, N.Y.) · 2011Article
- Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress.Nucleic acids research · 2010Article
- The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries.Molecular cell · 2009Article
- Metazoan stress granule assembly is mediated by P-eIF2alpha-dependent and -independent mechanisms.RNA (New York, N.Y.) · 2009Article
- Phosphorylation of the eukaryotic initiation factor 3f by cyclin-dependent kinase 11 during apoptosis.FEBS letters · 2009Article
- Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.Journal of molecular biology · 2009Article
- A novel class of mRNA-containing cytoplasmic granules are produced in response to UV-irradiation.Molecular biology of the cell · 2008Article
- Fission yeast mitogen-activated protein kinase Sty1 interacts with translation factors.Eukaryotic cell · 2008Article
- Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae.Molecular biology of the cell · 2007Article
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7 authors at 3 institutions in 1 country.
Funding
Abstract
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.
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