scholarly journals Visualization of Microtubule Growth in Cultured Neurons via the Use of EB3-GFP (End-Binding Protein 3-Green Fluorescent Protein)

2003 ◽  
Vol 23 (7) ◽  
pp. 2655-2664 ◽  
Author(s):  
Tatiana Stepanova ◽  
Jenny Slemmer ◽  
Casper C. Hoogenraad ◽  
Gideon Lansbergen ◽  
Bjorn Dortland ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Cultured Neurons ◽  
Microtubule Growth ◽  
Green Fluorescent

scholarly journals Tobacco Mosaic Virus Movement Protein Interacts with Green Fluorescent Protein-Tagged Microtubule End-Binding Protein 1

2008 ◽  
Vol 147 (2) ◽  
pp. 611-623 ◽  
Author(s):  
Katrin Brandner ◽  
Adrian Sambade ◽  
Emmanuel Boutant ◽  
Pascal Didier ◽  
Yves Mély ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Binding Protein ◽  
Virus Movement ◽  
Green Fluorescent

scholarly journals Arfophilins Are Dual Arf/Rab 11 Binding Proteins That Regulate Recycling Endosome Distribution and Are Related to Drosophila Nuclear Fallout

2003 ◽  
Vol 14 (7) ◽  
pp. 2908-2920 ◽  
Author(s):  
Gilles R.X. Hickson ◽  
Johanne Matheson ◽  
Blake Riggs ◽  
Valerie H. Maier ◽  
Andrew B. Fielding ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Binding Capacity ◽  
Binding Protein ◽  
Focal Adhesions ◽  
Dependent Manner ◽  
Recycling Endosome ◽  
Nuclear Fallout ◽  
Endosomal Recycling ◽  
Green Fluorescent

Arfophilin is an ADP ribosylation factor (Arf) binding protein of unknown function. It is identical to the Rab11 binding protein eferin/Rab11-FIP3, and we show it binds both Arf5 and Rab11. We describe a related protein, arfophilin-2, that interacts with Arf5 in a nucleotide-dependent manner, but not Arf1, 4, or 6 and also binds Rab11. Arfophilin-2 localized to a perinuclear compartment, the centrosomal area, and focal adhesions. The localization of arfophilin-2 to the perinuclear compartment was selectively blocked by overexpression of Arf5-T31N. In contrast, a green fluorescent protein-arfophilin-2 chimera or arfophilin-2 deletions were localized around the centrosome in a region that was also enriched for transferrin receptors and Rab11 but not early endosome markers, suggesting that the distribution of the endosomal recycling compartment was altered. The arfophilins belong to a conserved family that includes Drosophila melanogaster nuclear fallout, a centrosomal protein required for cellularization. Expression of green fluorescent protein-nuclear fallout in HeLa cells resulted in a similar phenotype, indicative of functional homology and thus implicating the arfophilins in mitosis/cytokinesis. We suggest that the novel dual GTPase-binding capacity of the arfophilins could serve as an interface of signals from Rab and Arf GTPases to regulate membrane traffic and integrate distinct signals in the late endosomal recycling compartment.

Monitoring of conformational change in maltose binding protein using split green fluorescent protein

2006 ◽  
Vol 339 (2) ◽  
pp. 647-651 ◽  
Author(s):  
Jinyoung Jeong ◽  
Sang Kyu Kim ◽  
Junhyoung Ahn ◽  
Kyoungsook Park ◽  
Eun-Ju Jeong ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Conformational Change ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Green Fluorescent

scholarly journals Toxofilin, a Novel Actin-binding Protein from Toxoplasma gondii, Sequesters Actin Monomers and Caps Actin Filaments

2000 ◽  
Vol 11 (1) ◽  
pp. 355-368 ◽  
Author(s):  
Olivier Poupel ◽  
Haralabia Boleti ◽  
Sophie Axisa ◽  
Evelyne Couture-Tosi ◽  
Isabelle Tardieux
Keyword(s):  
Green Fluorescent Protein ◽  
Toxoplasma Gondii ◽  
Host Cell ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Green Fluorescent

Toxoplasma gondii relies on its actin cytoskeleton to glide and enter its host cell. However, T. gondii tachyzoites are known to display a strikingly low amount of actin filaments, which suggests that sequestration of actin monomers could play a key role in parasite actin dynamics. We isolated a 27-kDa tachyzoite protein on the basis of its ability to bind muscle G-actin and demonstrated that it interacts with parasite G-actin. Cloning and sequence analysis of the gene coding for this protein, which we named Toxofilin, showed that it is a novel actin-binding protein. In in vitro assays, Toxofilin not only bound to G-actin and inhibited actin polymerization as an actin-sequestering protein but also slowed down F-actin disassembly through a filament end capping activity. In addition, when green fluorescent protein-tagged Toxofilin was overexpressed in mammalian nonmuscle cells, the dynamics of actin stress fibers was drastically impaired, whereas green fluorescent protein-Toxofilin copurified with G-actin. Finally, in motile parasites, during gliding or host cell entry, Toxofilin was localized in the entire cytoplasm, including the rear end of the parasite, whereas in intracellular tachyzoites, especially before they exit from the parasitophorous vacuole of their host cell, Toxofilin was found to be restricted to the apical end.

scholarly journals PBP1 Is a Component of the Bacillus subtilis Cell Division Machinery

2004 ◽  
Vol 186 (15) ◽  
pp. 5153-5156 ◽  
Author(s):  
Dirk-Jan Scheffers ◽  
Jeffery Errington
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Subtilis Cell ◽  
Knockout Strain ◽  
Green Fluorescent

ABSTRACT Bacillus subtilis penicillin-binding protein PBP1 has been implicated in cell division. We show here that a PBP1 knockout strain is affected in the formation of the asymmetric sporulation septum and that green fluorescent protein-PBP1 localizes to the sporulation septum. Localization of PBP1 to the vegetative septum is dependent on various cell division proteins. This study proves that PBP1 forms part of the B. subtilis cell division machinery.

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