The Subcellular Distribution of Eukaryotic Translation Initiation Factor, eIF-5A, in Cultured Cells

Shi, Xiao‐Ping; Yin, Kuo‐Chang; Zimolo, Z.; Stern, Andrew M.; Waxman, Lloyd

doi:10.1006/excr.1996.0185

Cited by 46 publications

(49 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Levels of the protein continued to increase between 24 and 72 h after infection, coincident with the progression of cell death in the infected leaves manifesting as diffuse chlorosis and necrotic lesions, which are the typical symptoms of virulent Pst DC3000-induced disease. That immunolabeled AteIF5A-2 protein colocalizes with TUNEL-positive nuclei in infected cells is consistent with the proposal emanating from studies with mammalian cells that eIF5A may function as a nucleocytoplasmic shuttle, recruiting and translocating specific mRNAs out of the nucleus into the cytoplasm for subsequent translation (Shi et al, 1996;Rosorius et al, 1999;Lipowsky et al, 2000;Jao and Chen, 2005). It is also consistent with reports that there is an accumulation of eIF5A within the nuclei of mammalian cells undergoing apoptosis Beninati et al, 1998;Caraglia et al, 2003;Jin et al, 2003;Taylor et al, 2007).…”

Section: Discussionsupporting

confidence: 86%

“…2). Because TUNEL labeling depicts fragmented DNA, this indicates that AteIF5A-2 is at least partially localized in nuclei and is consistent with mammalian cell studies signifying that eIF5A acts as a nucleocytoplasmic shuttling protein (Shi et al, 1996;Rosorius et al, 1999;Lipowsky et al, 2000;Jao and Chen, 2005). The incidence of TUNEL staining increased between 24 and 72 h after infection (Fig.…”

supporting

confidence: 86%

“…There is also evidence that eIF5A may play a role in apoptosis as it accumulates at the onset of cell death Beninati et al, 1998;Caraglia et al, 2003;Li et al, 2004;Taylor et al, 2007). The precise way in which eIF5A functions in cells is not known, but there are some reports based on studies with yeast and mammalian cells that it may selectively recruit specific subsets of mRNA from the nucleus, facilitating their translocation to the cytoplasm for subsequent translation (Shi et al, 1996;Rosorius et al, 1999;Lipowsky et al, 2000;Jao and Chen, 2005).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Eukaryotic Translation Initiation Factor 5A Is Involved in Pathogen-Induced Cell Death and Development of Disease Symptoms in Arabidopsis

et al. 2008

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 86%

supporting

confidence: 86%

mentioning

confidence: 99%

See 1 more Smart Citation

Eukaryotic Translation Initiation Factor 5A Is Involved in Pathogen-Induced Cell Death and Development of Disease Symptoms in Arabidopsis

et al. 2008

View full text Add to dashboard Cite

“…In accordance with these studies, we show here that eIF5A forms a physical complex with exportin1/CRM1 in a manner that is not hypusine dependent, and that hypusine is required for the functional export of Nos2 mRNA in conjunction with exportin1/CRM1. We recognize, however, that the nucleocytoplasmic shuttling of eIF5A has been challenged by other groups (43,44), and still others purport an interaction between eIF5A and exportin4 (46). We cannot exclude the possibility that exportin4 may also play a role in the transport of Nos2, considering that leptomycin B inhibition of exportin1/CRM1 blocked only approximately 50% of Nos2 export in our hands.…”

Section: Figure 10contrasting

confidence: 62%

The unique hypusine modification of eIF5A promotes islet β cell inflammation and dysfunction in mice

et al. 2010

View full text Add to dashboard Cite

In both type 1 and type 2 diabetes, pancreatic islet dysfunction results in part from cytokine-mediated inflammation. The ubiquitous eukaryotic translation initiation factor 5A (eIF5A), which is the only protein to contain the amino acid hypusine, contributes to the production of proinflammatory cytokines. We therefore investigated whether eIF5A participates in the inflammatory cascade leading to islet dysfunction during the development of diabetes. As described herein, we found that eIF5A regulates iNOS levels and that eIF5A depletion as well as the inhibition of hypusination protects against glucose intolerance in inflammatory mouse models of diabetes. We observed that following knockdown of eIF5A expression, mice were resistant to β cell loss and the development of hyperglycemia in the low-dose streptozotocin model of diabetes. The depletion of eIF5A led to impaired translation of iNOS-encoding mRNA within the islet. A role for the hypusine residue of eIF5A in islet inflammatory responses was suggested by the observation that inhibition of hypusine synthesis reduced translation of iNOS-encoding mRNA in rodent β cells and human islets and protected mice against the development of glucose intolerance the low-dose streptozotocin model of diabetes. Further analysis revealed that hypusine is required in part for nuclear export of iNOS-encoding mRNA, a process that involved the export protein exportin1. These observations identify the hypusine modification of eIF5A as a potential therapeutic target for preserving islet function under inflammatory conditions.

show abstract

“…However, subsequent studies have not confirmed the involvement of eIF5A with Rev-dependent nuclear export in either mammalian or yeast systems (Shi et al 1996(Shi et al , 1997Henderson and Percipalle 1997;Lipowsky et al 2000;Li-En Jao and Chen 2002;Valentini et al 2002). Moreover, the effect of eIF5A on mRNA decay seems to be secondary, as arrest of cell growth of eIF5A temperaturesensitive mutants does not directly correlate with mRNA accumulation (Valentini et al 2002).…”

mentioning

confidence: 99%

Pkc1 Acts Through Zds1 and Gic1 to Suppress Growth and Cell Polarity Defects of a Yeast eIF5A Mutant

Zanelli

Valentini

2005

Genetics

View full text Add to dashboard Cite

eIF5A is a highly conserved putative eukaryotic translation initiation factor that has been implicated in translation initiation, nucleocytoplasmic transport, mRNA decay, and cell proliferation, but with no precise function assigned so far. We have previously shown that high-copy PKC1 suppresses the phenotype of tif51A-1, a temperature-sensitive mutant of eIF5A in S. cerevisiae. Here, in an attempt to further understand how Pkc1 functionally interacts with eIF-5A, it was determined that PKC1 suppression of tif51A-1 is independent of the cell integrity MAP kinase cascade. Furthermore, two new suppressor genes, ZDS1 and GIC1, were identified. We demonstrated that ZDS1 and ZDS2 are necessary for PKC1, but not for GIC1 suppression. Moreover, high-copy GIC1 also suppresses the growth defect of a PKC1 mutant (stt1), suggesting the existence of a Pkc1-Zds1-Gic1 pathway. Consistent with the function of Gic1 in actin organization, the tif51A-1 strain shows an actin polarity defect that is partially recovered by overexpression of Pkc1 and Zds1 as well as Gic1. Additionally, PCL1 and BNI1, important regulators of yeast cell polarity, also suppress tif51A-1 temperature sensitivity. Taken together, these data strongly support the correlated involvement of Pkc1 and eIF5A in establishing actin polarity, which is essential for bud formation and G1/S transition in S. cerevisiae.

show abstract

The Subcellular Distribution of Eukaryotic Translation Initiation Factor, eIF-5A, in Cultured Cells

Cited by 46 publications

References 0 publications

Eukaryotic Translation Initiation Factor 5A Is Involved in Pathogen-Induced Cell Death and Development of Disease Symptoms in Arabidopsis

Eukaryotic Translation Initiation Factor 5A Is Involved in Pathogen-Induced Cell Death and Development of Disease Symptoms in Arabidopsis

The unique hypusine modification of eIF5A promotes islet β cell inflammation and dysfunction in mice

Pkc1 Acts Through Zds1 and Gic1 to Suppress Growth and Cell Polarity Defects of a Yeast eIF5A Mutant

Contact Info

Product

Resources

About