Synchronicity: policing multiple aspects of gene expression by Ctk1: Figure 1.

Hampsey, Michael; Kinzy, Terri Goss

doi:10.1101/gad.1564807

Cited by 6 publications

(4 citation statements)

References 39 publications

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“…Among the other strains with low levels of ceramides and IPC, one unsuspected mutant is ctk1Δ . CTK1 is a subunit of C-terminal domain kinase (CTDK-1) that is involved in transcriptional regulation and translational events ( Hampsey and Kinzy, 2007 ). Of interest, data from a phosphoproteomic study ( Bodenmiller et al.…”

Section: Resultsmentioning

confidence: 99%

Systematic lipidomic analysis of yeast protein kinase and phosphatase mutants reveals novel insights into regulation of lipid homeostasis

Santos

Riezman

Aguilera-Romero

et al. 2014

MBoC

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Section: Resultsmentioning

confidence: 99%

Systematic lipidomic analysis of yeast protein kinase and phosphatase mutants reveals novel insights into regulation of lipid homeostasis

Santos

Riezman

Aguilera-Romero

et al. 2014

MBoC

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“…Another scenario could be that efficient recruitment and stable binding of Aly to HSP70 mRNA require a second adaptor protein, such as Thoc5, that could stabilize the export receptor-cargo complex under heat shock, which may tend to destabilize protein complexes (e.g., Shukla et al, 1990). Finally, in light of the recent findings that transcription and translation can be coupled in eukaryotic cells (Hampsey and Kinzy, 2007;Marr II et al, 2007;Rother and Strasser, 2007), it is tempting to speculate that Thoc5 and/or components of the THO complex could have an additional function in HSP70 gene expression. The HSP70 mRNA is translated by a cap-independent mechanism due to an IRES (-like) activity within the 5 0 -untranslated region in higher eukaryotes (Klemenz et al, 1985;McGarry and Lindquist, 1985;Hultmark et al, 1986;Joshi and Nguyen, 1995;Hernandez et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA

Katahira

Inoue

Hurt

et al. 2009

EMBO J

133

183

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In metazoans, nuclear export of bulk mRNA is mediated by Tap-p15, a conserved heterodimeric export receptor that cooperates with adaptor RNA-binding proteins. In this article, we show that Thoc5, a subunit of the mammalian TREX complex, binds to a distinct surface on the middle (Ntf2-like) domain of Tap. Notably, adaptor protein Aly and Thoc5 can simultaneously bind to non-overlapping binding sites on Tap-p15. In vivo, Thoc5 was not required for bulk mRNA export. However, nuclear export of HSP70 mRNA depends on both Thoc5 and Aly. Consistent with a function as a specific export adaptor, Thoc5 exhibits in vitro RNA-binding activity and is associated with HSP70 mRNPs in vivo as a component of the stable THO complex. Thus, through the combinatorial use of an adaptor (e.g., Aly) and co-adapter (e.g., Thoc5), Tapp15 could function as an export receptor for different classes of mRNAs.

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“…The three genes encoding proteins of the CTDK-I complex (Ctk1, Ctk2, and Ctk3) are synthetically lethal with CDC34 tm (Figure 6, A and B; data not shown). The CTDK-1 complex coordinates transcriptional elongation, pre-mRNA 39-end processing, and translational fidelity (reviewed in Hampsey and Kinzy 2007). The role of CTDK-1 in transcriptional elongation is well characterized, and its ability to phosphorylate the second serine of the repetitive C-terminal domain of the largest subunit of Pol II (Rpo21) increases the efficiency of transcriptional elongation (Lee and Greenleaf 1997;Patturajan et al 1999).…”

Section: D103-114mentioning

confidence: 99%

New Insight Into the Role of the Cdc34 Ubiquitin-Conjugating Enzyme in Cell Cycle Regulation via Ace2 and Sic1

Cocklin¹,

Heyen²,

Larry

et al. 2011

Genetics

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The Cdc34 ubiquitin-conjugating enzyme plays a central role in progression of the cell cycle. Through analysis of the phenotype of a mutant missing a highly conserved sequence motif within the catalytic domain of Cdc34, we discovered previously unrecognized levels of regulation of the Ace2 transcription factor and the cyclin-dependent protein kinase inhibitor Sic1. In cells carrying the Cdc34 tm mutation, which alters the conserved sequence, the cyclin-dependent protein kinase inhibitor Sic1, an SCF Cdc4 substrate, has a shorter half-life, while the cyclin Cln1, an SCF Grr1 substrate, has a longer half-life than in wild-type cells. Expression of the SIC1 gene cluster, which is regulated by Swi5 and Ace2 transcription factors, is induced in CDC34 tm cells. Levels of Swi5, Ace2, and the SCF Grr1 targets Cln1 and Cln2 are elevated in Cdc34 tm cells, and loss of Grr1 causes an increase in Ace2 levels. Sic1 levels are similar in CDC34 tm ace2D and wild-type cells, explaining a paradoxical increase in the steady-state level of Sic1 protein despite its reduced half-life. A screen for mutations that interact with CDC34 tm uncovered novel regulators of Sic1, including genes encoding the polyubiquitin chain receptors Rad23 and Rpn10.

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Synchronicity: policing multiple aspects of gene expression by Ctk1: Figure 1.

Cited by 6 publications

References 39 publications

Systematic lipidomic analysis of yeast protein kinase and phosphatase mutants reveals novel insights into regulation of lipid homeostasis

Systematic lipidomic analysis of yeast protein kinase and phosphatase mutants reveals novel insights into regulation of lipid homeostasis

Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA

New Insight Into the Role of the Cdc34 Ubiquitin-Conjugating Enzyme in Cell Cycle Regulation via Ace2 and Sic1

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