Protein kinase C coordinates histone H3 phosphorylation and acetylation

Darieva, Zoulfia; Webber, Aaron; Warwood, Stacey; Sharrocks, Andrew D.

doi:10.7554/elife.09886

Cited by 17 publications

(11 citation statements)

References 42 publications

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“…In addition to transcription, evidence has been obtained that Pkc1 phosphorylates two nuclear targets that are necessary for efficient re-assembly of chromatin following DNA replication [ 240 ]. For this process, histone H3 (Hht1 and Hht2 in yeast) is phosphorylated at Thr46, which promotes its acetylation at Lys57.…”

Section: Substrates Of Pkc1mentioning

confidence: 99%

“…For this process, histone H3 (Hht1 and Hht2 in yeast) is phosphorylated at Thr46, which promotes its acetylation at Lys57. Under conditions of replicative stress, Pkc1 appears responsible for H3 T46 phosphorylation and Pkc1, by reportedly phosphorylating Thr46 (by coincidence at the same residue number) in the histone acetyltransferase Rtt109, also stimulates acetylation of H3 K57 [ 240 ]. The site in Hht1 (Hht2 is identical in sequence) matches some features of the pseudosubstrate sequence in Pkc1, whereas it matches the putative site in Rtt109 much less so ( Figure 7 ).…”

Section: Substrates Of Pkc1mentioning

confidence: 99%

“… Reported sites of Pkc1 phosphorylation. The evidence for Pkc1 phosphorylation of the indicated site (red) in the gene products listed (position of first residue in the sequence shown indicated on the left) can be found described in the following citations: Amp4 [ 237 ]; Bck1 [ 215 , 238 ]; Cdc55 [ 239 ]; Hht1 and Hht2 [ 240 ]; Igo2 [ 239 ]; Ndd1 [ 241 ]; Nem1 [ 233 ]; Pah1 [ 233 ]; Rtt109 [ 240 ]; Syp1 [ 242 ]; and, Ura7 [ 233 , 243 ]. …”

Section: Figurementioning

confidence: 99%

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The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae

et al. 2017

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To grow, eukaryotic cells must expand by inserting glycerolipids, sphingolipids, sterols, and proteins into their plasma membrane, and maintain the proper levels and bilayer distribution. A fungal cell must coordinate growth with enlargement of its cell wall. In Saccharomyces cerevisiae, a plasma membrane-localized protein kinase complex, Target of Rapamicin (TOR) complex-2 (TORC2) (mammalian ortholog is mTORC2), serves as a sensor and master regulator of these plasma membrane- and cell wall-associated events by directly phosphorylating and thereby stimulating the activity of two types of effector protein kinases: Ypk1 (mammalian ortholog is SGK1), along with a paralog (Ypk2); and, Pkc1 (mammalian ortholog is PKN2/PRK2). Ypk1 is a central regulator of pathways and processes required for plasma membrane lipid and protein homeostasis, and requires phosphorylation on its T-loop by eisosome-associated protein kinase Pkh1 (mammalian ortholog is PDK1) and a paralog (Pkh2). For cell survival under various stresses, Ypk1 function requires TORC2-mediated phosphorylation at multiple sites near its C terminus. Pkc1 controls diverse processes, especially cell wall synthesis and integrity. Pkc1 is also regulated by Pkh1- and TORC2-dependent phosphorylation, but, in addition, by interaction with Rho1-GTP and lipids phosphatidylserine (PtdSer) and diacylglycerol (DAG). We also describe here what is currently known about the downstream substrates modulated by Ypk1-mediated and Pkc1-mediated phosphorylation.

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Section: Substrates Of Pkc1mentioning

confidence: 99%

Section: Substrates Of Pkc1mentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae

et al. 2017

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“…It has been proposed that one protein modification might initiate the signaling that leads to the addition or removal of a second protein modification or the binding of another protein, suggesting that cross talk between protein modification components may serve as an important bypass of regulating protein functions. For example, both methylation and phosphorylation are able to trigger acetylation of histones [ 20 ].…”

Section: Cross Talk Among the Physiological Functional Components Of mentioning

confidence: 99%

N-myristoylation: from cell biology to translational medicine

et al. 2020

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Various lipids and lipid metabolites are bound to and modify the proteins in eukaryotic cells, which are known as ‘protein lipidation’. There are four major types of the protein lipidation, i.e. myristoylation, palmitoylation, prenylation, and glycosylphosphatidylinositol anchor. N-myristoylation refers to the attachment of 14-carbon fatty acid myristates to the N-terminal glycine of proteins by N-myristoyltransferases (NMT) and affects their physiology such as plasma targeting, subcellular tracking and localization, thereby influencing the function of proteins. With more novel pathogenic N-myristoylated proteins are identified, the N-myristoylation will attract great attentions in various human diseases including infectious diseases, parasitic diseases, and cancers. In this review, we summarize the current understanding of N-myristoylation in physiological processes and discuss the hitherto implication of crosstalk between N-myristoylation and other protein modification. Furthermore, we mention several well-studied NMT inhibitors mainly in infectious diseases and cancers and generalize the relation of NMT and cancer progression by browsing the clinic database. This review also aims to highlight the further investigation into the dynamic crosstalk of N-myristoylation in physiological processes as well as the potential application of protein N-myristoylation in translational medicine.

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“…Furthermore, the combination of H3Y41 and H3K56 function together can significantly increase the accessibility of DNA by more than an order of magnitude [ 29 ]. Histone H3 phosphorylated at threonines45 (H3T45) takes part in apoptosis and DNA replication and can promote the acetylation of H3K56 [ 30 , 31 ]. There is various kinase responsible for phosphorylation such as Aurora kinase(AKs), protein kinase B (PKB/Akt), cyclin-dependent kinases (CDKs), protein kinase C (PKC), casein kinase 2 (Ck2) and Rad3 related kinase ATR [ 32 ], and so on.…”

Section: Histone Modificationmentioning

confidence: 99%

Histone Modifications and their Role in Colorectal Cancer (Review)

Qin

Wen

Liang

et al. 2019

Pathol. Oncol. Res.

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The development of colorectal cancer is a complex and multistep process mediated by a variety of factors including the dysregulation of genetic and epigenetic under the influence of microenvironment. It is evident that epigenetics that affects gene activity and expression has been recognized as a critical role in the carcinogenesis. Aside from DNA methylation, miRNA level, and genomic imprinting, histone modification is increasingly recognized as an essential mechanism underlying the occurrence and development of colorectal cancer. Aberrant regulation of histone modification like acetylation, methylation and phosphorylation levels on specific residues is implicated in a wide spectrum of cancers, including colorectal cancer. In addition, as this process is reversible and accompanied by a plethora of deregulated enzymes, inhibiting those histone-modifying enzymes activity and regulating its level has been thought of as a potential path for tumor therapy. This review provides insight into the basic information of histone modification and its application in the colorectal cancer treatment, thereby offering new potential targets for treatment of colorectal cancer.

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Protein kinase C coordinates histone H3 phosphorylation and acetylation

Cited by 17 publications

References 42 publications

The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae

The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae

N-myristoylation: from cell biology to translational medicine

Histone Modifications and their Role in Colorectal Cancer (Review)

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