Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)-Based Quantitative Proteomics and Phosphoproteomics in Fission Yeast

Autor: Weronika E. Borek, Kenneth E. Sawin, Boris Macek, Claudia C. Bicho, Alejandro Carpy, André Koch, Silke Hauf

Publikováno v: Cold Spring Harbor Protocols. 2017:pdb.prot091686

Modern mass spectrometry (MS)-based approaches are capable of identifying and quantifying thousands of proteins and phosphorylation events in a single biological experiment. Here we present a (phospho)proteomic workflow based on in-solution proteome

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a003018ce50542dac3353d096e6417b8
https://doi.org/10.1101/pdb.prot091686

Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial control of cytokinesis

Autor: Sergio A. Rincón, Weronika E. Borek, Kenneth E. Sawin, Flavia de Lima Alves, Vincent Fraisier, Mercè Guzman-Vendrell, Anne Paoletti, Sophie G. Martin, Damarys Loew, Payal Bhatia, Claudia C. Bicho, Juri Rappsilber, Florent Dingli

Publikováno v: Rincon, S A, Bhatia, P, Bicho, C, Guzman-Vendrell, M, Fraisier, V, Borek, W E, Alves, F D L, Dingli, F, Loew, D, Rappsilber, J, Sawin, K E, Martin, S G & Paoletti, A 2014, ' Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial control of cytokinesis ', Journal of Cell Biology, vol. 206, no. 1, pp. 61-77 . https://doi.org/10.1083/jcb.201311097
Journal of Cell Biology, vol. 206, no. 1, pp. 61-77
The Journal of Cell Biology

Pom1 regulation of Cdr2 membrane association and interaction with Mid1 prevents Cdr2 assembly into stable nodes in the cell tip region, which ensures proper positioning of cytokinetic ring precursors and accurate division plane positioning in fission

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ea9d32419d3b299622f325a46f79bfe
https://www.pure.ed.ac.uk/ws/files/17409894/61.full.pdf

A catalytic role for Mod5 in the formation of the Tea1 cell polarity landmark

Autor: Kenneth E. Sawin, David A. Kelly, Hilary A. Snaith, Andrew B. Goryachev, Claudia C. Bicho

Publikováno v: Current Biology
Bicho, C C, Kelly, D A, Snaith, H A, Goryachev, A B & Sawin, K E 2010, ' A Catalytic Role for Mod5 in the Formation of the Tea1 Cell Polarity Landmark ', Current Biology, vol. 20, no. 19, pp. 1752-1757 . https://doi.org/10.1016/j.cub.2010.08.035

Summary Many systems regulating cell polarity involve stable landmarks defined by internal cues [1–5]. In the rod-shaped fission yeast Schizosaccharomyces pombe, microtubules regulate polarized vegetative growth via a landmark involving the protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::443dfa6778da6e0615ee2df179755aa2
https://pubmed.ncbi.nlm.nih.gov/20850323

Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial control of cytokinesis.

Autor: Rincon SA; Centre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, France Centre National de la Recherche Scientifique, Unite Mixte de Recherche 144, F-75248 Paris, France., Bhatia P; Department of Fundamental Microbiology, University of Lausanne, Lausanne CH-1015, Switzerland., Bicho C; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, UK., Guzman-Vendrell M; Centre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, France Centre National de la Recherche Scientifique, Unite Mixte de Recherche 144, F-75248 Paris, France., Fraisier V; Centre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, France Centre National de la Recherche Scientifique, Unite Mixte de Recherche 144, F-75248 Paris, France., Borek WE; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, UK., Alves Fde L; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, UK., Dingli F; Centre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, FranceCentre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, France., Loew D; Centre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, FranceCentre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, France., Rappsilber J; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, UK., Sawin KE; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, UK., Martin SG; Department of Fundamental Microbiology, University of Lausanne, Lausanne CH-1015, Switzerland., Paoletti A; Centre de Recherche and Laboratory of Mass Spectrometry and Proteomics, Institut Curie, F-75248 Paris, France Centre National de la Recherche Scientifique, Unite Mixte de Recherche 144, F-75248 Paris, France anne.paoletti@curie.fr.

Publikováno v: The Journal of cell biology [J Cell Biol] 2014 Jul 07; Vol. 206 (1), pp. 61-77. Date of Electronic Publication: 2014 Jun 30.