Evidence that Yih1 resides in a complex with ribosomes

Waller, Tracey; Lee, Su Jung; Sattlegger, Evelyn

doi:10.1111/j.1742-4658.2012.08553.x

Cited by 17 publications

(20 citation statements)

References 36 publications

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“…The mechanism that drives IMPACT molecules to associate with polysomes upon differentiation remains to be determined. The polysomal association of Yih1 in yeast has been recently demonstrated (41). Our data then further support the functional similarities of the two orthologs.…”

Section: Discussionsupporting

confidence: 83%

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IMPACT Is a Developmentally Regulated Protein in Neurons That Opposes the Eukaryotic Initiation Factor 2α Kinase GCN2 in the modulation of Neurite Outgrowth

Roffé

Hajj²,

Azevedo

et al. 2013

Journal of Biological Chemistry

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Background: IMPACT inhibits GCN2, a kinase that directs stress remedial responses by attenuating translation and controls feeding behavior and memory. Results: Neuronal IMPACT is developmentally up-regulated, promoting protein synthesis and neuritogenesis, opposing GCN2. Conclusion: GCN2 and IMPACT modulate an early step in neuronal differentiation. Significance: A neuron-specific developmental program is controlled by two evolutionarily conserved translational regulators.

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Section: Discussionsupporting

confidence: 83%

“…This observation suggests that IMPACT may disrupt GCN1-GCN2 interaction on polysomes without GCN2 release. In fact, it has been demonstrated in yeast that Yih1 overexpression does not displace GCN2 from ribosomes (41). GCN1 distribution remained unchanged after differentiation; and when considering the reduction in poly- …”

Section: Discussionmentioning

confidence: 97%

IMPACT Is a Developmentally Regulated Protein in Neurons That Opposes the Eukaryotic Initiation Factor 2α Kinase GCN2 in the modulation of Neurite Outgrowth

Roffé

Hajj²,

Azevedo

et al. 2013

Journal of Biological Chemistry

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“…Yih1p is not a generic or constitutive Gcn2p inhibitor, but instead appears to down-regulate Gcn2p activity only under certain conditions and/or in specific locations in the cell (e.g., when or where it is not associated with G-actin) [198]. Yih1p was found to associate with ribosomes as found for Gcn1p and Gcn2p, suggesting that this allows instant Gcn2p inhibition at the site where Gcn2p senses the starvation signal and reversal of inhibition [232]. Therefore, one can envision that due to the changing dynamics of actin filament assembly and disassembly, the actin cytoskeleton spatiotemporally determines the amount of Yih1p that is available to dampen Gcn2p activation.…”

Section: Regulation Of Gcn2 By Yih1p/impact and The Link To Actinmentioning

confidence: 90%

Yeast as a Model to Understand Actin-Mediated Cellular Functions in Mammals—Illustrated with Four Actin Cytoskeleton Proteins

Akram

Ahmed

Mack

et al. 2020

Cells

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The budding yeast Saccharomyces cerevisiae has an actin cytoskeleton that comprises a set of protein components analogous to those found in the actin cytoskeletons of higher eukaryotes. Furthermore, the actin cytoskeletons of S. cerevisiae and of higher eukaryotes have some similar physiological roles. The genetic tractability of budding yeast and the availability of a stable haploid cell type facilitates the application of molecular genetic approaches to assign functions to the various actin cytoskeleton components. This has provided information that is in general complementary to that provided by studies of the equivalent proteins of higher eukaryotes and hence has enabled a more complete view of the role of these proteins. Several human functional homologues of yeast actin effectors are implicated in diseases. A better understanding of the molecular mechanisms underpinning the functions of these proteins is critical to develop improved therapeutic strategies. In this article we chose as examples four evolutionarily conserved proteins that associate with the actin cytoskeleton: (1) yeast Hof1p/mammalian PSTPIP1, (2) yeast Rvs167p/mammalian BIN1, (3) yeast eEF1A/eEF1A1 and eEF1A2 and (4) yeast Yih1p/mammalian IMPACT. We compare the knowledge on the functions of these actin cytoskeleton-associated proteins that has arisen from studies of their homologues in yeast with information that has been obtained from in vivo studies using live animals or in vitro studies using cultured animal cell lines.

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“…In vivo association of proteins with polyribosomes was determined as described previously [25]. Briefly, yeast cells were grown to exponential phase in 300 ml of SC (synthetic complete) medium to an A 600 of ∼1 in 1-l baffled flasks.…”

Section: Ribosome Co-sedimentation Assaysmentioning

confidence: 99%

Gcn1 contacts the small ribosomal protein Rps10, which is required for full activation of the protein kinase Gcn2

Lee

Swanson

Sattlegger

2015

Biochemical Journal

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In eukaryotes, amino acid deprivation leads to the accumulation of uncharged tRNAs that are detected by Gcn2 (general control non-derepressible 2), which in turn phosphorylates eIF2α (α-subunit of eukaryotic translation initiation factor 2), an essential process for overcoming starvation. In Saccharomyces cerevisiae, sensing amino acid shortages requires that Gcn2 binds directly to its effector protein Gcn1 and both must associate with the ribosome. Our hypothesis is that uncharged tRNAs occur in the ribosomal A-site and that Gcn1 is directly involved in transfer of this starvation signal to Gcn2. In the present paper, we provide evidence that Gcn1 directly contacts the small ribosomal protein S10 (Rps10). Gcn1 residues 1060-1777 showed a yeast two-hybrid (Y2H) interaction with Rps10A. In vitro, Rps10A or Rps10B co-precipitated Gcn1[1060-1777] in an RNA-independent manner. rps10AΔ or rps10BΔ strains showed reduced eIF2α phosphorylation under replete conditions and shortly after onset of starvation, suggesting that Gcn1-mediated Gcn2 activation was impaired. Overexpression of GST-tagged Rps10 reduced growth under amino acid starvation and this was exacerbated by the Gcn1-M7A mutation known to impair Gcn1-ribosome interaction and Gcn2 activity. Under amino acid starvation, eEF3 (eukaryotic translation elongation factor 3) overexpression, known to weaken Gcn1 function on the ribosome, exacerbated the growth defect of rps10AΔ or rps10BΔ strains. Taken together, these data support the idea that Gcn1 contacts ribosome-bound Rps10 to efficiently mediate Gcn2 activation.

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Evidence that Yih1 resides in a complex with ribosomes

Cited by 17 publications

References 36 publications

IMPACT Is a Developmentally Regulated Protein in Neurons That Opposes the Eukaryotic Initiation Factor 2α Kinase GCN2 in the modulation of Neurite Outgrowth

IMPACT Is a Developmentally Regulated Protein in Neurons That Opposes the Eukaryotic Initiation Factor 2α Kinase GCN2 in the modulation of Neurite Outgrowth

Yeast as a Model to Understand Actin-Mediated Cellular Functions in Mammals—Illustrated with Four Actin Cytoskeleton Proteins

Gcn1 contacts the small ribosomal protein Rps10, which is required for full activation of the protein kinase Gcn2

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