Combining Protein-Based IMAC, Peptide-Based IMAC, and MudPIT for Efficient Phosphoproteomic Analysis

Cantin, Greg T.; Yi, Wei; Lu, Bingwen; Park, Sung Kyu; Xu, Tao; Lee, Jiing-Dwan; Yates, John R.

doi:10.1021/pr0705441

Cited by 139 publications

(148 citation statements)

References 26 publications

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“…In some cases, definitive localization of the phosphorylation site could not be obtained (Figure 1a, sites marked in green). Some of these sites have previously been reported, including Ser21 and Ser1177, which have been identified in different largescale analyses of phosphoproteins (Beausoleil et al, 2004;Dai et al, 2007;Cantin et al, 2008;Daub et al, 2008;Dephoure et al, 2008;Zanivan et al, 2008). In addition, the phosphopeptides containing Ser1174, Ser1219, Thr1222, Thr1295, Ser1385, Tyr1386 and Ser1388, which have recently reported been, were also detected (Dephoure et al, 2008;Zanivan et al, 2008).…”

Section: Identification Of Phosphorylation Sites Within Rictormentioning

confidence: 70%

Rictor is a novel target of p70 S6 kinase-1

et al. 2009

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The rapamycin-insensitive companion of mammalian target of rapamycin (mTOR) (Rictor) is a key member of mTOR complex-2 (mTORC2), which phosphorylates the AGC kinases Akt/PKB, PKC and SGK1 at a C-terminal hydrophobic motif. We identified several novel sites on Rictor that are phosphorylated, including Thr1135, which is conserved across all vertebrates. Phosphorylation of this site on Rictor is stimulated by amino acids and growth factors through a rapamycin-sensitive signaling cascade. We demonstrate here that Rictor is a direct target of the ribosomal protein S6 kinase-1 (S6K1). Rictor phosphorylation at Thr1135 does not lead to major changes in mTORC2-kinase activity. However, phosphorylation of this site turns over rapidly and mediates 14-3-3 binding to Rictor and mTORC2, providing possibility for altered interactions of the complex. These findings reveal an unexpected signaling input into mTORC2, which is regulated by amino acids, growth factors and rapamycin.

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Section: Identification Of Phosphorylation Sites Within Rictormentioning

confidence: 70%

Rictor is a novel target of p70 S6 kinase-1

et al. 2009

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“…MYBBP1A is reported to be a heavily phosphorylated protein in cells, according to several recent large scale mass spectrometry-based phosphoproteomic studies (65)(66)(67)(68)(69)(70)(71)(72). The majority of the phosphorylation sites mapped in MYBBP1A in these studies (18 of a total of 21) reside within the ϳ200-amino acid-long C-terminal portion of the protein, which has been shown to be relevant for its nuclear and nucleolar localization (73).…”

Section: Discussionmentioning

confidence: 99%

Identification of Myb-binding Protein 1A (MYBBP1A) as a Novel Substrate for Aurora B Kinase

Perrera

Colombo

Valsasina

et al. 2010

Journal of Biological Chemistry

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Aurora kinases are mitotic enzymes involved in centrosome maturation and separation, spindle assembly and stability, and chromosome condensation, segregation, and cytokinesis and represent well known targets for cancer therapy because their deregulation has been linked to tumorigenesis. The availability of suitable markers is of crucial importance to investigate the functions of Auroras and monitor kinase inhibition in in vivo models and in clinical trials. Extending the knowledge on Aurora substrates could help to better understand their biology and could be a source for clinical biomarkers. Using biochemical, mass spectrometric, and cellular approaches, we identified MYBBP1A as a novel Aurora B substrate and serine 1303 as the major phosphorylation site. MYBBP1A is phosphorylated in nocodazole-arrested cells and is dephosphorylated upon Aurora B silencing or by treatment with Danusertib, a small molecule inhibitor of Aurora kinases. Furthermore, we show that MYBBP1A depletion by RNA interference causes mitotic progression delay and spindle assembly defects. MYBBP1A has until now been described as a nucleolar protein, mainly involved in transcriptional regulation. The results presented herein show MYBBP1A as a novel Aurora B kinase substrate and reveal a not yet recognized link of this nucleolar protein to mitosis.

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“…EGF stimulates phosphorylation at Ser-54, Ser-58, Ser-171, and Ser-173) (106,107). S54F is a "special" EDMD-causing mutation that does not disrupt emerin expression or localization yet still causes EDMD (78).…”

Section: Discussionmentioning

confidence: 99%

O-Linked β-N-Acetylglucosamine (O-GlcNAc) Regulates Emerin Binding to Barrier to Autointegration Factor (BAF) in a Chromatin- and Lamin B-enriched “Niche”

Berk

Maitra

Dawdy

et al. 2013

Journal of Biological Chemistry

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Background: Nuclear membrane protein emerin binding to nuclear intermediate filaments (lamins) and BAF contributes to forming a nuclear "lamina" structure. Results: Emerin is O-GlcNAc-modified at eight sites: two (Ser-53 and Ser-54) influence further O-GlcNAcylation, and one (Ser-173) regulates association with BAF in the chromatin/lamin B "niche." Conclusion: O-GlcNAc transferase, a nutrient-responsive enzyme, regulates emerin. Significance: Emerin hyper-O-GlcNAcylation may contribute to cardiomyopathy and other conditions.

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Combining Protein-Based IMAC, Peptide-Based IMAC, and MudPIT for Efficient Phosphoproteomic Analysis

Cited by 139 publications

References 26 publications

Rictor is a novel target of p70 S6 kinase-1

Rictor is a novel target of p70 S6 kinase-1

Identification of Myb-binding Protein 1A (MYBBP1A) as a Novel Substrate for Aurora B Kinase

O-Linked β-N-Acetylglucosamine (O-GlcNAc) Regulates Emerin Binding to Barrier to Autointegration Factor (BAF) in a Chromatin- and Lamin B-enriched “Niche”

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