Pheromone-Dependent Destruction of the Tec1 Transcription Factor Is Required for MAP Kinase Signaling Specificity in Yeast

Bao, Marie Z.; Schwartz, Monica A.; Cantin, Greg T.; Yates, John R.; Madhani, Hiten D.

doi:10.1016/j.cell.2004.11.052

Cited by 139 publications

(141 citation statements)

References 32 publications

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“…Alternatively, posttranslational modifications to Vg or Sd (or both) may modify their activity. Interestingly, the yeast Sd homologue, Tec1, is phosphorylated and then degraded during the mating pheromone response (Bao et al, 2004). In mammals, TEF-1 is phosphorylated responding to cAMP/PK-A signaling (Gupta et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Alternative Requirements for Vestigial, Scalloped, and Dmef2 during Muscle Differentiation inDrosophila melanogaster

Deng

Hughes

Bell³

et al. 2009

MBoC

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Vertebrate development requires the activity of the myocyte enhancer factor 2 (mef2) gene family for muscle cell specification and subsequent differentiation. Additionally, several muscle-specific functions of MEF2 family proteins require binding additional cofactors including members of the Transcription Enhancing Factor-1 (TEF-1) and Vestigiallike protein families. In Drosophila there is a single mef2 (Dmef2) gene as well single homologues of TEF-1 and vestigial-like, scalloped (sd), and vestigial (vg), respectively. To clarify the role(s) of these factors, we examined the requirements for Vg and Sd during Drosophila muscle specification. We found that both are required for muscle differentiation as loss of sd or vg leads to a reproducible loss of a subset of either cardiac or somatic muscle cells in developing embryos. This muscle requirement for Sd or Vg is cell specific, as ubiquitous overexpression of either or both of these proteins in muscle cells has a deleterious effect on muscle differentiation. Finally, using both in vitro and in vivo binding assays, we determined that Sd, Vg, and Dmef2 can interact directly. Thus, the muscle-specific phenotypes we have associated with Vg or Sd may be a consequence of alternative binding of Vg and/or Sd to Dmef2 forming alternative protein complexes that modify Dmef2 activity. INTRODUCTIONSpecification and differentiation of both vertebrate and invertebrate muscles requires a conserved cohort of transcription factors (Baylies et al., 1998;Cripps and Olson, 2002). Among these, myocyte enhancer factor-2 (MEF2) plays a key role in specification and subsequent differentiation of all muscle types (skeletal, smooth, and heart muscle; Lilly et al., 1995;. There are four different known vertebrate mef2 genes: mef2-a, -b, -c, and -d (Black and Olson, 1998). These four genes produce several different MEF2 isoforms involved in differentiation of all muscle types. In addition, it has been proposed that MEF2 proteins have a requirement for tissue-specific cofactors to confer additional specificity. For example, during mammalian heart development, GATA-4 (Charron and Nemer, 1999) helps to recruit MEF2 to the promoters of cardiac-specific genes including atrial natriuretic factor (ANF) and ␣-cardiac actin (␣-CA; Morin et al., 2000). MEF2 also interacts with another transcription factor, HAND1, during activation of ANF in cardiac cells (Morin et al., 2005). This complex interplay between MEF2 proteins and cofactors is not restricted to cardiac muscles as during skeletal muscle development; MEF2 interacts with MyoD during activation of specific structural genes (Molkentin et al., 1995;.In terms of MEF2 protein family activity, muscle differentiation in Drosophila is relatively less complex as there is only a single homologue mef2, Dmef2 (Lilly et al., 1994). Like vertebrates, Drosophila Dmef2 isoforms activate muscle-specific genes and also seems to interact with a conserved cohort of interacting proteins for muscle specification, including cardiogenesis. These include tinman (Azp...

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Section: Discussionmentioning

confidence: 99%

Alternative Requirements for Vestigial, Scalloped, and Dmef2 during Muscle Differentiation inDrosophila melanogaster

Deng

Hughes

Bell³

et al. 2009

MBoC

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“…Dia2 has recently been proposed to target a transcription factor in the pheromone-response pathway for ubiquitination (Bao et al, 2004), although this conclusion is controversial (Chou et al, 2004). Other evidence suggests that Dia2 plays a role in cell cycle progression.…”

Section: Introductionmentioning

confidence: 99%

“…It has recently been proposed that Tec1, a pheromone-responsive transcription factor involved in the filamentous growth pathway, is a substrate of SCF Dia2 (Bao et al, 2004). Although it is formally possible that the role of Dia2 in the filamentation pathway is linked to the DNA replication timing defects in dia2 mutants, we think these pathways are independent as the dia2 clb5 clb6 mutant still exhibits the elongated cell/bipolar budding pattern phenotype.…”

Section: Other Roles For Scf Dia2mentioning

confidence: 99%

The F-Box Protein Dia2 Regulates DNA Replication

Koepp

Kile

Swaminathan

et al. 2006

MBoC

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Ubiquitin-mediated proteolysis plays a key role in many pathways inside the cell and is particularly important in regulating cell cycle transitions. SCF (Skp1/Cul1/F-box protein) complexes are modular ubiquitin ligases whose specificity is determined by a substrate-binding F-box protein. Dia2 is a Saccharomyces cerevisiae F-box protein previously described to play a role in invasive growth and pheromone response pathways. We find that deletion of DIA2 renders cells cold-sensitive and subject to defects in cell cycle progression, including premature S-phase entry. Consistent with a role in regulating DNA replication, the Dia2 protein binds replication origins. Furthermore, the dia2 mutant accumulates DNA damage in both S and G2/M phases of the cell cycle. These defects are likely a result of the absence of SCF Dia2 activity, as a Dia2 ⌬F-box mutant shows similar phenotypes. Interestingly, prolonging G1-phase in dia2 cells prevents the accumulation of DNA damage in S-phase. We propose that Dia2 is an origin-binding protein that plays a role in regulating DNA replication.

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“…In this regard, the Fus3-regulated pheromone-dependent destruction of Tec1, a transcription factor involved in filamentous response, determines MAPK signalling specificity. Removal of any key element participating in this ubiquitinmediated regulation results in erroneous filamentation pathway gene expression and invasive growth as a consequence of mating pathway activation [2,9].…”

Section: Ubiquitination In Mapk-mediated Signalling: No Longer Forgetmentioning

confidence: 99%

Fine regulation of Saccharomyces cerevisiae MAPK pathways by post‐translational modifications

Molina

Cid

Martı́n

2010

Yeast

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Saccharomyces cerevisiae has been widely used as a model eukaryotic organism to elucidate the molecular mechanisms that operate upon activation of signalling pathways. For over two decades, many clues to the regulation of mitogen-activated protein kinase (MAPK) pathways have derived from basic research in yeast. Here we review aspects of MAPK pathway fine-tuning, such as the functional implication of feedback loops or regulatory inputs from other pathways, mediated by post-transcriptional modifications on their components. The impact of recent phosphoproteomic approaches in this particular field is also discussed.

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Pheromone-Dependent Destruction of the Tec1 Transcription Factor Is Required for MAP Kinase Signaling Specificity in Yeast

Cited by 139 publications

References 32 publications

Alternative Requirements for Vestigial, Scalloped, and Dmef2 during Muscle Differentiation inDrosophila melanogaster

Alternative Requirements for Vestigial, Scalloped, and Dmef2 during Muscle Differentiation inDrosophila melanogaster

The F-Box Protein Dia2 Regulates DNA Replication

Fine regulation of Saccharomyces cerevisiae MAPK pathways by post‐translational modifications

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