Cell cycle-dependent O-GlcNAc modification of tobacco histones and their interaction with the tobacco lectin

Delporte, Annelies; Zaeytijd, Jeroen De; Storme, Nico De; Azmi, Abdelkrim; Geelen, Danny; Smagghe, Guy; Guisez, Yves; Damme, Els J.M. Van

doi:10.1016/j.plaphy.2014.07.021

Cited by 25 publications

(20 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Phosphorylation of the CTD is required and precedes elongation (151). O-GlcNAc is part of the histone code (152)(153)(154)(155)(156)(157)(158)(159). Whereas several O-GlcNAc sites on histones are in the tail regions, along with other epigenetic marks, some ASBMB AWARD ARTICLE: Regulation of signaling and transcription O-GlcNAc moieties are located at the histone:DNA interface.…”

Section: Nutrient Regulation Of Gene Expressionmentioning

confidence: 99%

Nutrient regulation of signaling and transcription

Hart

2019

Journal of Biological Chemistry

288

225

View full text Add to dashboard Cite

O‐GlcNAc cycles on and off thousands of nucleocytoplasmic proteins and has extensive crosstalk with protein phosphorylation. O‐GlcNAc cycles on nearly all proteins involved in transcription, where it regulates gene expression in response to nutrients. O‐GlcNAc also regulates the cycling of the TATA‐binding (TBP) protein on and off DNA during the transcription cycle. Targeted, inducible, deletion of the O‐GlcNAc Transferase (OGT) in aCAMKII positive (excitatory) neurons of adult mice results in a morbidly obese mouse with a satiety defect. Thus, O‐GlcNAcylation not only serves as a nutrient sensor in all cells, but also is directly involved in appetite regulation. O‐GlcNAcylation also plays an important role in the trafficking of the AMPA receptors in neurons and in the development of functional synaptic spines. Recent studies have shown that more than one‐half of all human protein kinases are modified by O‐GlcNAc and all kinases that have been tested are indeed regulated in some way by the sugar. Abnormal O‐GlcNAcylation of CAMKII contributes directly to diabetic cardiomyopathy and to arrhythmias associated with diabetes. Prolonged elevation of O‐GlcNAc, as occurs in diabetes, contributes directly to diabetic complications and is a major mechanism of glucose toxicity. Drugs that elevate O‐GlcNAcylation in the brain, which, in‐turn, prevents hyperphosphorylation, appear to be of benefit for the treatment of Alzheimer's disease in animal models. To date, all cancers have elevated O‐GlcNAc cycling, which may play a key role in the regulation of metabolism in cancer cells. Support or Funding Information Supported by NIH P01HL107153, R01GM116891, R01DK61671, and N01‐HV‐00240. Dr. Hart receives a share of royalty received by the university on sales of the CTD 110.6 antibody, which are managed by JHU. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.

show abstract

Section: Nutrient Regulation Of Gene Expressionmentioning

confidence: 99%

Nutrient regulation of signaling and transcription

Hart

2019

Journal of Biological Chemistry

288

225

View full text Add to dashboard Cite

show abstract

“…During DNA synthesis in S-phase, the newly formed DNA strand is loaded onto histone proteins, and histones, including H1, H2A, H2B, H3, and H4, are O-GlcNAcylated [25,30–32]. A histone octamer is composed of two copies of the four core histone proteins, namely H2A, H2B, H3, and H4 [33].…”

Section: O-glcnac Cycling In Interphasementioning

confidence: 99%

“…This process is regulated by histone phosphorylation, methylation, and acetylation at different phases of the cell cycle. Interestingly, histone H3 O-GlcNAcylation steadily rises into G 2 ; however, when the cell transitions into M-phase, the H3 O-GlcNAcylation level declines gradually [32]. Histone H1 O-GlcNAcylation increases at the beginning of M-phase only to decline in the late M-phase in Nicotiana tabacum [32].…”

Section: O-glcnac Cycling In Interphasementioning

confidence: 99%

“…Interestingly, histone H3 O-GlcNAcylation steadily rises into G 2 ; however, when the cell transitions into M-phase, the H3 O-GlcNAcylation level declines gradually [32]. Histone H1 O-GlcNAcylation increases at the beginning of M-phase only to decline in the late M-phase in Nicotiana tabacum [32]. Similarly in mammalian cells, histone H3 O-GlcNAcylation significantly declines at the G 2 /M transition [30].…”

Section: O-glcnac Cycling In Interphasementioning

confidence: 99%

See 1 more Smart Citation

The sweet side of the cell cycle

Tan

Duncan

Slawson

2017

Biochemical Society Transactions

View full text Add to dashboard Cite

Cell division (mitosis) and gamete production (meiosis) are fundamental requirements for normal organismal development. The mammalian cell cycle is tightly regulated by different checkpoints ensuring complete and precise chromosomal segregation and duplication. In recent years, researchers have become increasingly interested in understanding how O-GlcNAc regulates the cell cycle. The O-GlcNAc post-translation modification is an O-glycosidic bond of a single β-N-acetylglucosamine sugar to serine/threonine residues of intracellular proteins. This modification is sensitive toward changes in nutrient levels in the cellular environment making O-GlcNAc a nutrient sensor capable of influencing cell growth and proliferation. Numerous studies have established that O-GlcNAcylation is essential in regulating mitosis and meiosis, while loss of O-GlcNAcylation is lethal in growing cells. Moreover, aberrant O-GlcNAcylation is linked with cancer and chromosomal segregation errors. In this review, we will discuss how O-GlcNAc controls different aspects of the cell cycle with a particular emphasis on mitosis and meiosis.

show abstract

“…For a long time, the capsid protein (CP) of Plum pox virus (PPV), which is modified by SEC, was the only protein definitively identified as a natural target of a specific plant OGT (Chen et al, 2005). Although there is sound evidence of functionally relevant O-GlcNAcylation in several plant proteins, such as the Nicotiana tabacum non-cellautonomous pathway protein 1 (Nt-NCAPP1) and some phloem non-cell-autonomous proteins (NCAPs) of pumpkin (Taoka et al, 2007), two A. thaliana TCP transcription factors, TCP14 and TCP15 (Steiner et al, 2012), some lectin-interacting tobacco histones (Delporte et al, 2014;Schouppe et al, 2011) and the vernalization-related RNA-binding protein TaGRP2 of wheat (Xiao et al, 2014;Xing et al, 2009), the OGTs involved in these putative modifications have not been identified. Recently, SECmediated O-GlcNAcylation of several proteins of the DELLA family of transcription regulators has been demonstrated in Arabidopsis (Zentella et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation coexists with O‐GlcNAcylation in a plant virus protein and influences viral infection

Martínez-Turiño

Pérez

Hervás

et al. 2018

Molecular Plant Pathology

View full text Add to dashboard Cite

Phosphorylation and O-GlcNAcylation are two widespread post-translational modifications (PTMs), often affecting the same eukaryotic target protein. Plum pox virus (PPV) is a member of the genus Potyvirus which infects a wide range of plant species. O-GlcNAcylation of the capsid protein (CP) of PPV has been studied extensively, and some evidence of CP phosphorylation has also been reported. Here, we use proteomics analyses to demonstrate that PPV CP is phosphorylated in vivo at the N-terminus and the beginning of the core region. In contrast with the 'yin-yang' mechanism that applies to some mammalian proteins, PPV CP phosphorylation affects residues different from those that are O-GlcNAcylated (serines Ser-25, Ser-81, Ser-101 and Ser-118). Our findings show that PPV CP can be concurrently phosphorylated and O-GlcNAcylated at nearby residues. However, an analysis using a differential proteomics strategy based on iTRAQ (isobaric tags for relative and absolute quantitation) showed a significant enhancement of phosphorylation at Ser-25 in virions recovered from O-GlcNAcylation-deficient plants, suggesting that crosstalk between O-GlcNAcylation and phosphorylation in PPV CP takes place. Although the preclusion of phosphorylation at the four identified phosphotarget sites only had a limited impact on viral infection, the mimicking of phosphorylation prevents PPV infection in Prunus persica and weakens infection in Nicotiana benthamiana and other herbaceous hosts, prompting the emergence of potentially compensatory second mutations. We postulate that the joint action of phosphorylation and O-GlcNAcylation in the N-proximal segment of CP allows a fine-tuning of protein stability, providing the amount of CP required in each step of viral infection.

show abstract

Cell cycle-dependent O-GlcNAc modification of tobacco histones and their interaction with the tobacco lectin

Cited by 25 publications

References 34 publications

Nutrient regulation of signaling and transcription

Nutrient regulation of signaling and transcription

The sweet side of the cell cycle

Phosphorylation coexists with O‐GlcNAcylation in a plant virus protein and influences viral infection

Contact Info

Product

Resources

About