Výsledky vyhledávání - "Nick A. Morrice"

Akademický článek

Massive autophosphorylation of the Ser/Thr-rich domain controls protein kinase activity of TRPM6 and TRPM7.

Autor: Kristopher Clark, Jeroen Middelbeek, Nick A Morrice, Carl G Figdor, Edwin Lasonder, Frank N van Leeuwen

Publikováno v: PLoS ONE, Vol 3, Iss 3, p e1876 (2008)

TRPM6 and TRPM7 are bifunctional proteins expressing a TRP channel fused to an atypical alpha-kinase domain. While the gating properties of TRPM6 and TRPM7 channels have been studied in detail, little is known about the mechanisms regulating kinase a

Externí odkaz: https://doaj.org/article/7698f9dc761844ae84244a5b619b0d9f

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Deciphering the Dark Proteome: Use of the Testis and Characterization of Two Dark Proteins

Autor: Régis Lavigne, Laetitia Guillot, Mélanie Lagarrigue, Pascale Bellaud, Emmanuelle Com, Jörg Dojahn, Juan-Felipe Velez de la Calle, Charles Pineau, Blandine Guével, Nick A. Morrice, Nathalie Melaine

Publikováno v: Journal of Proteome Research
Journal of Proteome Research, American Chemical Society, 2018, 44 (1), pp.13-30. ⟨10.1021/acs.jproteome.8b00387⟩
Journal of Proteome Research, 2018, 44 (1), pp.13-30. ⟨10.1021/acs.jproteome.8b00387⟩
BASE-Bielefeld Academic Search Engine

For the C-HPP consortium, dark proteins include not only uPE1, but also missing proteins (MPs, PE2-4), smORFs, proteins from lncRNAs, and products from uncharacterized transcripts. Here, we investigated the expression of dark proteins in the human te

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3587da1b50212f810218fe44bef4067c
https://pubmed.ncbi.nlm.nih.gov/30130116

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PP2AT61ɛ Is an Inhibitor of MAP4K3 in Nutrient Signaling to mTOR

Autor: Greg M. Findlay, Lijun Yan, Virginie Mieulet, Nick A. Morrice, Jozef Goris, Katherine Sully, Julia Procter, Veerle Janssens, Richard F. Lamb, Darren J. Burgess

Publikováno v: Molecular Cell. 37(5):633-642

The mammalian target of rapamycin (mTOR) pathway is activated by a variety of stimuli, including nutrients such as glucose and amino acids. The Ste20 family kinase MAP4K3 is regulated by amino acids and acts upstream of mTORC1. Here we investigate ho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f30375764a28130d3ac67f9e01df3e9a

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Regulation of the Interaction between Protein Kinase C-related Protein Kinase 2 (PRK2) and Its Upstream Kinase, 3-Phosphoinositide-dependent Protein Kinase 1 (PDK1)

Autor: Matthias Engel, Stefan Zeuzem, Ricardo M. Biondi, Lucas Meyer, L.A. Lopez-Garcia, Silvina Sonzogni, Morten Frödin, Sonja Neimanis, Nick A. Morrice, Albrecht Piiper, Rosalia Dettori

Publikováno v: Journal of Biological Chemistry. 284:30318-30327

The members of the AGC kinase family frequently exhibit three conserved phosphorylation sites: the activation loop, the hydrophobic motif (HM), and the zipper (Z)/turn-motif (TM) phosphorylation site. 3-Phosphoinositide-dependent protein kinase 1 (PD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dcf02f99c93f296be4a02532cfcb4be
https://doi.org/10.1074/jbc.m109.051151

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Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators

Autor: Carol MacKintosh, Nick A. Morrice, Jane Murphy, Shuai Chen, David G. Campbell, Rachel Toth

Publikováno v: Biochemical Journal. 409:449-459

AS160 (Akt substrate of 160 kDa) and TBC1D1 are related RabGAPs (Rab GTPase-activating proteins) implicated in regulating the trafficking of GLUT4 (glucose transporter 4) storage vesicles to the cell surface. All animal species examined contain TBC1D

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5137fb45196943f9931d9b6be803f1c5
https://doi.org/10.1042/bj20071114

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Identification of novel phosphorylation sites in MSK1 by precursor ion scanning MS

Autor: Andrew Macdonald, Nick A. Morrice, J. Simon C. Arthur, David G. Campbell, Maria Deak, Joanne McIlrath, Claire E. McCoy, Rachel Toth

Publikováno v: Biochemical Journal. 402:491-501

MSK1 (mitogen- and stress-activated kinase 1) is a dual kinase domain protein that acts downstream of the ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38 MAPK (mitogen-activated protein kinase) signalling pathways in cells. MSK1, and its r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff291bd272834f4ce9782c2850bfa5b
https://doi.org/10.1042/bj20061183

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Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress

Autor: Alberto C. Vitari, Anna Zagórska, Jérôme Boudeau, Nick A. Morrice, David G. Campbell, Jacob Thastrup, Dario R. Alessi, Alan R. Prescott, Eulalia Pozo-Guisado, Maria Deak, Fatema H. Rafiqi

Publikováno v: The Journal of Cell Biology

Mutations within the WNK1 (with-no-K[Lys] kinase-1) gene cause Gordon's hypertension syndrome. Little is known about how WNK1 is regulated. We demonstrate that WNK1 is rapidly activated and phosphorylated at multiple residues after exposure of cells

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a586c9fe06cbcd866e8edc98d5ef83a
https://doi.org/10.1083/jcb.200605093

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Pim Kinase Substrate Identification and Specificity

Autor: Axel Knebel, Charline Peng, Brian Werneburg, Xiang Li, Scott Jakes, Kevin Barringer, Jun Li, Lian Wang, Nick A. Morrice

Publikováno v: Journal of Biochemistry. 141:353-362

The Pim family of Ser/Thr kinases has been implicated in the process of lymphomagenesis and cell survival. Known substrates of Pim kinases are few and poorly characterized. In this study we set out to identify novel Pim-2 substrates using the Kinase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97157313f740542d3bb6e3e2b03b7699
https://doi.org/10.1093/jb/mvm040

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Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylation

Autor: Stephan Wullschleger, Maria Deak, Alan R. Prescott, Dario R. Alessi, Nick A. Morrice, Olga Göransson

Publikováno v: Journal of Cell Science. 119:4059-4070

Members of the PAR-1/MARK kinase family play critical roles in polarity and cell cycle control and are regulated by 14-3-3 scaffolding proteins, as well as the LKB1 tumour suppressor kinase and atypical protein kinase C (PKC). In this study, we initi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::272d8c4f0a4a769940709a3db61be06f
https://doi.org/10.1242/jcs.03097

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14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK

Autor: Alan R. Prescott, Rachel Toth, Dario R. Alessi, Olga Göransson, David G. Campbell, Nick A. Morrice, Maria Deak, Abdallah Al-Hakim

Publikováno v: Journal of Cell Science. 118:5661-5673

The LKB1 tumour suppressor kinase phosphorylates and activates a number of protein kinases belonging to the AMP-activated protein kinase (AMPK) subfamily. We have used a modified tandem affinity purification strategy to identify proteins that interac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c8f59ee18fca2b533dd94d344d0a290
https://doi.org/10.1242/jcs.02670

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