Cell cycle control of the yeast HO gene: Cis- and Trans-acting regulators

Breeden, Linda; Nasmyth, Kim

doi:10.1016/0092-8674(87)90190-5

Cited by 376 publications

(294 citation statements)

References 39 publications

Supporting

Mentioning

287

Contrasting

Order By: Relevance

“…b-galactosidase filter and liquid culture assays, using as substrates 5-brom-4-chlor-3-indoxyl-b-D-galactoside (X-gal) and o-nitrophenyl b-D-galactopyranoside (ON�G), respectively, were performed as described. 24 b-galactosidase values represent mean numbers and standard deviations of three independent experiments.…”

Section: Methodsmentioning

confidence: 99%

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G₂/M Genes

Schmit¹,

Korenjak²,

Mannefeld³

et al. 2007

Cell Cycle

176

247

View full text Add to dashboard Cite

Here we report the identification of the LIN complex (LINC), a human multiprotein complex that is required for transcriptional activation of G 2 /M genes. LINC is related to the recently identified dREAM and DRM complexes of Drosophila and C. elegans that contain homologs of the mammalian retinoblastoma tumor suppressor protein. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC dynamically associates with pocket proteins, E2F and B-MYB during the cell cycle. In quiescent cells, LINC binds to p130 and E2F4. During cell cycle entry, E2F4 and p130 dissociate and LINC switches to B-MYB and p107. Chromatin Immunoprecipitation experiments demonstrate that LINC associates with a large number of E2F-regulated promoters in quiescent cells. However, RNAi experiments reveal that LINC is not required for repression. In S-phase, LINC selectively binds to the promoters of G 2 /M genes whose products are required for mitosis and plays an important role in their cell cycle dependent activation.

show abstract

Section: Methodsmentioning

confidence: 99%

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G₂/M Genes

Schmit¹,

Korenjak²,

Mannefeld³

et al. 2007

Cell Cycle

176

247

View full text Add to dashboard Cite

show abstract

“…Growth and manipulation of yeast were carried out according to standard procedures (Adams et al 1997). ␤-Galactosidase expression in the two-hybrid strain CTY10-5D (Bartel and Fields 1995) was measured both by liquid assay (Moretti et al 1994) and by nitrocellulose filter assay (Breeden and Nasmyth 1987). Plasmids carrying LexA-Pol12 (full-length) fusion hybrids were obtained by cloning XmaI-XhoI DNA fragments containing either POL12 or pol12-216 genes in the XmaI-SalI-digested pBTM116 vector (Bartel and Fields 1995; pGS86 and pGS96, respectively).…”

Section: Yeast Strains Media and Plasmidsmentioning

confidence: 99%

Pol12, the B subunit of DNA polymerase α, functions in both telomere capping and length regulation

Grossi¹,

Puglisi²,

Dmitriev³

et al. 2004

Genes Dev.

129

173

View full text Add to dashboard Cite

The regulation of telomerase action, and its coordination with conventional DNA replication and chromosome end "capping," are still poorly understood. Here we describe a genetic screen in yeast for mutants with relaxed telomere length regulation, and the identification of Pol12, the B subunit of the DNA polymerase ␣ (Pol1)-primase complex, as a new factor involved in this process. Unlike many POL1 and POL12 mutations, which also cause telomere elongation, the pol12-216 mutation described here does not lead to either reduced Pol1 function, increased telomeric single-stranded DNA, or a reduction in telomeric gene silencing. Instead, and again unlike mutations affecting POL1, pol12-216 is lethal in combination with a mutation in the telomere end-binding and capping protein Stn1. Significantly, Pol12 and Stn1 interact in both two-hybrid and biochemical assays, and their synthetic-lethal interaction appears to be caused, at least in part, by a loss of telomere capping. These data reveal a novel function for Pol12 and a new connection between DNA polymerase ␣ and Stn1. We propose that Pol12, together with Stn1, plays a key role in linking telomerase action with the completion of lagging strand synthesis, and in a regulatory step required for telomere capping.

show abstract

“…The solution ␤-galactosidase assays were performed as described (35), and the units of ␤-galactosidase activity were calculated by the method of Miller (36).…”

Section: Methodsmentioning

confidence: 99%

Interaction of MAD2 with the Carboxyl Terminus of the Insulin Receptor but Not with the IGFIR EVIDENCE FOR RELEASE FROM THE INSULIN RECEPTOR AFTER ACTIVATION

O’Neill

Zhu

Gustafson

1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

We have utilized the yeast two-hybrid system to identify proteins that interact with the cytoplasmic domain of the insulin receptor (IR). We identified a human cDNA encoding a protein that appears to be the human homolog of the yeast MAD2 protein, which we term hMAD2. The yeast MAD2 protein was first identified in a genetic screen to identify cell cycle checkpoint regulatory proteins, yet the mechanism by which MAD2 functions in cell cycle control is currently unclear. Here we show that hMAD2 requires the COOH-terminal 30 amino acids of the IR for interaction and that hMAD2 does not interact with the related insulin-like growth factor I receptor. Interestingly, hMAD2 does not require IR tyrosine autophosphorylation for interaction because it interacts with a kinase-dead IR in the yeast two-hybrid system. In support of this finding, hMAD2-GST fusions were found to interact strongly in vitro with receptors derived from noninsulin-stimulated cells. Furthermore, using two independent in vitro assays, IR activation was found to significantly reduce the interaction of hMAD2 with the IR. Lastly, we show that hMAD2 can be coimmunoprecipitated with the IR from Chinese hamster ovary IR cell lysates, suggesting that this interaction occurs in vivo in cells of mammalian origin. Our results suggest that hMAD2 represents a novel class of proteins that is specific for interaction with the IR as compared with the insulin-like growth factor I receptor and that interacts best with the inactive IR and is released upon receptor autophosphorylation. The function of hMAD2 and its potential role in insulin signaling remain to be elucidated.Insulin regulates a large number of diverse effects within its target tissues. These effects include regulation of metabolic responses such as glucose transporter translocation and regulation of metabolic enzymes such as glycogen synthetase (1). In addition, many other cellular effects are thought to be regulated by insulin, including regulation of amino acid uptake, regulation of a number of enzymes involved in protein and lipid synthesis, and regulation of ion transport (1, 2). These effects are mediated through the insulin receptor (IR) 1 receptor tyrosine kinase. Like other receptor tyrosine kinases, the IR becomes phosphorylated upon tyrosines after insulin binding via an autophosphorylation cascade (3). Phosphorylation of particular tyrosines within the IR leads to the formation of binding sites for a variety of substrates and effector proteins. The best studied of these is the insulin receptor substrate 1 (IRS-1) (4, 5), which interacts with the juxtamembrane domain of the IR containing an NPXpY motif. This interaction requires phosphorylation of the tyrosine located within the NPXY motif (amino acid 960), 2 which has been shown to be critical for many insulindependent effects (6). Interaction of IRS-1 with the NPX(p)Y motif depends upon the phosphotyrosine binding domain located within the amino terminus of IRS-1 (7-9). Interaction of IRS-1 with the IR is believed to result in the phosphoryl...

show abstract

Cell cycle control of the yeast HO gene: Cis- and Trans-acting regulators

Cited by 376 publications

References 39 publications

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G₂/M Genes

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G₂/M Genes

Pol12, the B subunit of DNA polymerase α, functions in both telomere capping and length regulation

Interaction of MAD2 with the Carboxyl Terminus of the Insulin Receptor but Not with the IGFIR EVIDENCE FOR RELEASE FROM THE INSULIN RECEPTOR AFTER ACTIVATION

Contact Info

Product

Resources

About

Cell cycle control of the yeast HO gene: Cis- and Trans-acting regulators

Cited by 376 publications

References 39 publications

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G2/M Genes

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G2/M Genes

Pol12, the B subunit of DNA polymerase α, functions in both telomere capping and length regulation

Interaction of MAD2 with the Carboxyl Terminus of the Insulin Receptor but Not with the IGFIR EVIDENCE FOR RELEASE FROM THE INSULIN RECEPTOR AFTER ACTIVATION

Contact Info

Product

Resources

About

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G₂/M Genes

LINC, a Human Complex That is Related to pRB-Containing Complexes in Invertebrates Regulates the Expression of G₂/M Genes