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Your search keyword '"Jacob, Peter"' showing total 30 results
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30 results on '"Jacob, Peter"'

1. Ward monitoring 4.0: real-time metabolic insights from continuous glucose monitoring into perioperative organ dysfunction

Author

Janssen, Henrike, primary, Jhanji, Shaman, additional, Oliver, Nick S., additional, Ackland, Gareth L., additional, Korbonits, Marta, additional, Henson, Sian, additional, Yeung, Joyce, additional, Pearse, Rupert, additional, Shelley, Ben, additional, Hiller, Louise, additional, Jacob, Peter, additional, Noblet, James, additional, Jefford, Monica, additional, Gutierrez del Arroyo, Ana, additional, Samman, Abeer, additional, Alharbi, Saja, additional, Ahuja, Sanjali, additional, and Dias, Priya, additional

Published
2024
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5. Identification and Characterization of MCM3 as a Kelch-like ECH-associated Protein 1 (KEAP1) Substrate

Author

Timothy M. Jacobs, Erica W. Cloer, Jacob Peter Matson, Jeanette Gowen Cook, Tigist Y. Tamir, Cyrus Vaziri, Priscila F. Siesser, Dennis Goldfarb, Michael B. Major, Joseph S. Harrison, and Kathleen M. Mulvaney

Subjects
Models, Molecular, 0301 basic medicine, Protein subunit, Biology, Proteomics, Biochemistry, Cell Line, Mice, 03 medical and health sciences, Ubiquitin, Autophagy, Animals, Humans, Protein Interaction Maps, Molecular Biology, Transcription factor, Kelch-Like ECH-Associated Protein 1, Cell Cycle, Ubiquitination, Minichromosome Maintenance Complex Component 3, Signal transducing adaptor protein, Cell Biology, Cullin Proteins, Molecular biology, Chromatin, Ubiquitin ligase, Cell biology, HEK293 Cells, 030104 developmental biology, biology.protein, Carrier Proteins, HeLa Cells, Signal Transduction
Abstract

KEAP1 is a substrate adaptor protein for a CUL3-based E3 ubiquitin ligase. Ubiquitylation and degradation of the antioxidant transcription factor NRF2 is considered the primary function of KEAP1; however, few other KEAP1 substrates have been identified. Because KEAP1 is altered in a number of human pathologies and has been proposed as a potential therapeutic target therein, we sought to better understand KEAP1 through systematic identification of its substrates. Toward this goal, we combined parallel affinity capture proteomics and candidate-based approaches. Substrate-trapping proteomics yielded NRF2 and the related transcription factor NRF1 as KEAP1 substrates. Our targeted investigation of KEAP1-interacting proteins revealed MCM3, an essential subunit of the replicative DNA helicase, as a new substrate. We show that MCM3 is ubiquitylated by the KEAP1-CUL3-RBX1 complex in cells and in vitro. Using ubiquitin remnant profiling, we identify the sites of KEAP1-dependent ubiquitylation in MCM3, and these sites are on predicted exposed surfaces of the MCM2–7 complex. Unexpectedly, we determined that KEAP1 does not regulate total MCM3 protein stability or subcellular localization. Our analysis of a KEAP1 targeting motif in MCM3 suggests that MCM3 is a point of direct contact between KEAP1 and the MCM hexamer. Moreover, KEAP1 associates with chromatin in a cell cycle-dependent fashion with kinetics similar to the MCM2–7 complex. KEAP1 is thus poised to affect MCM2–7 dynamics or function rather than MCM3 abundance. Together, these data establish new functions for KEAP1 within the nucleus and identify MCM3 as a novel substrate of the KEAP1-CUL3-RBX1 E3 ligase.

Published
2016
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6. Static and dynamic protein phosphorylation in the Vaccinia virion

Author

Wayne Chou, Jacob Peter Matson, Paul D. Gershon, and Tuan Ngo

Subjects
Kinase, Mass spectrometry, biology, Phosphopeptide, Molecular Sequence Data, Cyclin-dependent kinase 2, Virion, Vaccinia virus, Phosphoproteins, Molecular biology, Viral Proteins, Membrane protein, Biochemistry, Phosphoprotein, Virology, Vaccinia, biology.protein, Humans, Phosphorylation, Protein phosphorylation, Amino Acid Sequence, Protein kinase A
Abstract

To the best of our knowledge, two phosphorylation sites have been reported previously, among 11 known Vaccinia virus phosphoproteins. Here, via phosphopeptide mass spectrometry, up to 189 phosphorylation sites were identified among 48 proteins in preparations of purified Vaccinia mature virus (MV). 8.5% of phospho-residues were pTyr. Viral phosphoproteins were found in diverse functional classes, including structural proteins, membrane proteins and RNA polymerase subunits. Among the nine identified membrane phosphoproteins, the sites in just one, namely A14L, were deduced to be internal with respect to the accompanying membrane. Examination of sites in known substrates of the Vaccinia-encoded protein kinase VPK2, indicated VPK2 to be a proline-dependent kinase. The MV phosphoproteome was enriched in potential substrates of cellular kinases belonging to the CDK2/CDK3, CK2, and p38 groups. Quantitative mass spectrometry identified several sites that became phosphorylated during intravirion kinase activation in vitro, each showing one of two distinct pH-dependency profiles.

Published
2014
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