scholarly journals Reversible Optogenetic Control of Subcellular Protein Localization in a Live Vertebrate Embryo

2016 ◽  
Vol 36 (1) ◽  
pp. 117-126 ◽  
Author(s):  
Clare E. Buckley ◽  
Rachel E. Moore ◽  
Anna Reade ◽  
Anna R. Goldberg ◽  
Orion D. Weiner ◽  
...  
Keyword(s):  
Protein Localization ◽  
Subcellular Protein Localization ◽  
Vertebrate Embryo ◽  
Optogenetic Control

TheArabidopsis Localizome: Subcellular Protein Localization and Interactions inARABIDOPSIS

2008 ◽  
pp. 61-81
Author(s):  
Georgios Kitsios ◽  
Nicolas Tsesmetzis ◽  
Max Bush ◽  
John H. Doonan
Keyword(s):  
Protein Localization ◽  
Subcellular Protein Localization

scholarly journals MultiLoc2: integrating phylogeny and Gene Ontology terms improves subcellular protein localization prediction

2009 ◽  
Vol 10 (1) ◽  
Author(s):  
Torsten Blum ◽  
Sebastian Briesemeister ◽  
Oliver Kohlbacher
Keyword(s):  
Gene Ontology ◽  
Protein Localization ◽  
Subcellular Protein Localization ◽  
Localization Prediction

Barcodes for subcellular protein localization

2019 ◽  
Vol 3 (9) ◽  
pp. 673-675 ◽  
Author(s):  
Yizhe Zhang ◽  
Alden Moss ◽  
Kristine Tan ◽  
Amy E. Herr
Keyword(s):  
Protein Localization ◽  
Subcellular Protein Localization

scholarly journals High-throughput subcellular protein localization using cell arrays

2005 ◽  
Vol 33 (6) ◽  
pp. 1407 ◽  
Author(s):  
D. Vanhecke ◽  
Y.-H. Hu ◽  
H. Lehrach ◽  
M. Janitz
Keyword(s):  
High Throughput ◽  
Protein Localization ◽  
Subcellular Protein Localization ◽  
Cell Arrays

scholarly journals Glycolytic flux-signaling controls mouse embryo mesoderm development

2021 ◽  
Author(s):  
Hidenobu Miyazawa ◽  
Marteinn T. Snaebjornsson ◽  
Nicole Prior ◽  
Eleni Kafkia ◽  
Henrik M Hammarén ◽  
...  
Keyword(s):  
Soluble Fraction ◽  
Protein Localization ◽  
Proteome Analysis ◽  
Glycolytic Flux ◽  
Mesoderm Development ◽  
Subcellular Protein Localization ◽  
Fructose 1,6 Bisphosphate ◽  
Post Implantation ◽  
Medium Supplementation

How cellular metabolic state impacts cellular programs is a fundamental, unresolved question. Here we investigated how glycolytic flux impacts embryonic development, using presomitic mesoderm (PSM) patterning as the experimental model. First, we identified fructose 1,6-bisphosphate (FBP) as an in vivo sentinel metabolite that mirrors glycolytic flux within PSM cells of post-implantation mouse embryos. We found that medium-supplementation with FBP, but not with other glycolytic metabolites, such as fructose 6-phosphate and 3-phosphoglycerate, impaired mesoderm segmentation. To genetically manipulate glycolytic flux and FBP levels, we generated a mouse model enabling the conditional overexpression of dominant active, cytoplasmic Pfkfb3 (cytoPfkfb3). Overexpression of cytoPfkfb3 indeed led to increased glycolytic flux/FBP levels and caused an impairment of mesoderm segmentation, paralleled by the downregulation of Wnt-signaling, reminiscent of the effects seen upon FBP-supplementation. To probe for mechanisms underlying glycolytic flux-signaling, we performed subcellular proteome analysis and revealed that cytoPfkfb3 overexpression altered subcellular localization of certain proteins, including glycolytic enzymes, in PSM cells. Specifically, we revealed that FBP supplementation caused depletion of Pfkl and Aldoa from the nuclear-soluble fraction. Combined, we propose that FBP functions as a flux-signaling metabolite connecting glycolysis and PSM patterning, potentially through modulating subcellular protein localization.

scholarly journals Dynamic Patterns of Subcellular Protein Localization during Spore Coat Morphogenesis in Bacillus subtilis

2004 ◽  
Vol 186 (14) ◽  
pp. 4441-4448 ◽  
Author(s):  
Christiaan van Ooij ◽  
Patrick Eichenberger ◽  
Richard Losick
Keyword(s):  
Bacillus Subtilis ◽  
Subcellular Localization ◽  
Fluorescent Protein ◽  
Protein Localization ◽  
Distinct Pattern ◽  
Spore Coat ◽  
Short Axis ◽  
Subcellular Protein Localization ◽  
Associated Proteins ◽  
Green Fluorescent

ABSTRACT Endospores of Bacillus subtilis are encased in a thick, proteinaceous shell known as the coat, which is composed of a large number of different proteins. Here we report the identification of three previously uncharacterized coat-associated proteins, YabP, YheD, and YutH, and their patterns of subcellular localization during the process of sporulation, obtained by using fusions of the proteins to the green fluorescent protein (GFP). YabP-GFP was found to form both a shell and a ring around the center of the forespore across the short axis of the sporangium. YheD-GFP, in contrast, formed two rings around the forespore that were offset from its midpoint, before it eventually redistributed to form a shell around the developing spore. Finally, YutH-GFP initially localized to a focus at one end of the forespore, which then underwent transformation into a ring that was located adjacent to the forespore. Next, the ring became a cap at the mother cell pole of the forespore that eventually spread around the entire developing spore. Thus, each protein exhibited its own distinct pattern of subcellular localization during the course of coat morphogenesis. We concluded that spore coat assembly is a dynamic process involving diverse patterns of protein assembly and localization.

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