An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome

Bian, Yangyang; Song, Chunxia; Cheng, Kai; Dong, Mingming; Wang, Fangjun; Huang, Junfeng; Sun, Da; Wang, Liming; Ye, Mingliang; Zou, Hanfa

doi:10.1016/j.jprot.2013.11.014

Cited by 218 publications

(181 citation statements)

References 48 publications

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“…Both traditional and highthroughput proteomic investigations have identified variants of Ub phosphorylated at nearly all of its serine, threonine, or tyrosine resides [40]. This includes observations of pUb S20 [41][42][43], in humans, mice, and rats [3][4][5][6]. Ours is the first report of Ub phosphorylation sites (distinct from pS65) that modulate the activity of an E3 ligase.…”

Section: Codon Skippingmentioning

confidence: 81%

“…Parkin's substrate Ub was recently found to have at least seven experimentally observed phosphorylation sites in human cells [3][4][5][6]. As a result of the discovery of an upstream kinase, PTEN-induced putative kinase I (PINK1) [7], specific for Ub Ser65, a series of studies followed that show phosphorylation at Ser65 in Ub stimulates parkin's auto-ubiquitination activity [8][9][10][11][12].…”

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confidence: 99%

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Generation of phospho‐ubiquitin variants by orthogonal translation reveals codon skipping

et al. 2016

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Edited by Michael IbbaThe activity of the Parkinson's disease-linked E3 ligase parkin is stimulated by phosphorylation at ubiquitin Ser65 (pUb S65 ). The role of other ubiquitin phospho-sites and their kinases are unknown. We produced pUb variants (pS7, pS12, pS20, pS57, pS65) by genetically encoding phosphoserine with the UAG codon. In release factor-deficient Escherichia coli (DRF1), intended to enhance UAG read-through, we discovered ubiquitin variants lacking the UAG-encoded residue, demonstrating previously undocumented +3 frame shifting. We successfully purified each pUb variant from mistranslated products. While pUb S20 failed to stimulate parkin, parkin was partially active with pUb S12 . We observed significant ubiquitination when pUb S65 was the sole substrate.

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Section: Codon Skippingmentioning

confidence: 81%

mentioning

confidence: 99%

Generation of phospho‐ubiquitin variants by orthogonal translation reveals codon skipping

et al. 2016

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“…However, phosphorylated peptides of peroxisomal matrix proteins like ACOX1, ACOX3, MFE2, peroxisomal 3-ketoacyl-CoA thiolase, DHAPAT and catalase were regularly identified in the human and mouse phosphoproteome screens. In terms of membrane associated proteins, the peroxins Pex1 and Pex14, and to a lesser extent Pex11β/γ are potentially phosphorylated [9,24,117,120,124,180,186,192]. In addition, phosphorylation of the two peroxisomal ABC transporters involved in fatty acid import, ABCD1 and ABCD3, has been described [159].…”

Section: Defining the Peroxisomal Phosphoproteome -The Status Quomentioning

confidence: 99%

Proliferation and fission of peroxisomes — An update

Schrader

Costello

Godinho

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

119

140

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In mammals, peroxisomes perform crucial functions in cellular metabolism, signalling and viral defense which are essential to the health and viability of the organism. In order to achieve this functional versatility peroxisomes dynamically respond to molecular cues triggered by changes in the cellular environment. Such changes elicit a corresponding response in peroxisomes, which manifests itself as a change in peroxisome number, altered enzyme levels and adaptations to the peroxisomal structure. In mammals the generation of new peroxisomes is a complex process which has clear analogies to mitochondria, with both sharing the same division machinery and undergoing a similar division process. How the regulation of this division process is integrated into the cell's response to different stimuli, the signalling pathways and factors involved, remains somewhat unclear. Here, we discuss the mechanism of peroxisomal fission, the contributions of the various division factors and examine the potential impact of post-translational modifications, such as phosphorylation, on the proliferation process. We also summarize the signalling process and highlight the most recent data linking signalling pathways with peroxisome proliferation.

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“…Previous studies have shown that TG2 is phosphorylated by PKA at Ser 215 and Ser 216 [52] and at an unknown site(s) by PTEN-induced putative kinase 1 (PINK1; [53]). Phosphoproteomic based studies have identified numerous phosphorylation sites on Ser, Thr and Tyr residues in human and rat TG2 [54][55][56][57][58][59][60]. It would therefore be of value to identify the specific site(s) of TG2-associated serine and threonine phosphorylation triggered by the A1 adenosine receptor.…”

Section: A1 Adenosine Receptor-induced Phosphorylation Of Tg2mentioning

confidence: 99%

A1 adenosine receptor-induced phosphorylation and modulation of transglutaminase 2 activity in H9c2 cells: A role in cell survival

Vyas

Hargreaves

Bonner

et al. 2016

Biochemical Pharmacology

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The regulation of tissue transglutaminase (TG2) activity by the GPCR family is poorly understood. In this study, we investigated the modulation of TG2 activity by the A1 adenosine receptor in cardiomyocyte-like H9c2 cells.H9c2 cells were lysed following stimulation with the A1 adenosine receptor agonist N 6 -cyclopentyladenosine (CPA).Transglutaminase activity was determined using an amine incorporating and a protein cross linking assay. TG2 phosphorylation was assessed via immunoprecipitation and 3

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An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome

Cited by 218 publications

References 48 publications

Generation of phospho‐ubiquitin variants by orthogonal translation reveals codon skipping

Generation of phospho‐ubiquitin variants by orthogonal translation reveals codon skipping

Proliferation and fission of peroxisomes — An update

A1 adenosine receptor-induced phosphorylation and modulation of transglutaminase 2 activity in H9c2 cells: A role in cell survival

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