scholarly journals When a Day Makes a Difference. Interpreting Data from Endoplasmic Reticulum-Targeted Green Fluorescent Protein Fusions in Cells Grown in Suspension Culture

2002 ◽  
Vol 128 (2) ◽  
pp. 341-344 ◽  
Author(s):  
Staffan Persson ◽  
John Love ◽  
Pei-Lan Tsou ◽  
Dominique Robertson ◽  
William F. Thompson ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Green Fluorescent Protein ◽  
Suspension Culture ◽  
Fluorescent Protein ◽  
Green Fluorescent ◽  
In Cells

Increased Redox-Sensitive Green Fluorescent Protein Reduction Potential in the Endoplasmic Reticulum following Glutathione-Mediated Dimerization

Biochemistry ◽  
2013 ◽  
Vol 52 (19) ◽  
pp. 3332-3345 ◽  
Author(s):  
Deboleena Dipak Sarkar ◽  
Sarah K. Edwards ◽  
Justin A. Mauser ◽  
Allen M. Suarez ◽  
Maxwell A. Serowoky ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Green Fluorescent Protein ◽  
Reduction Potential ◽  
Fluorescent Protein ◽  
Green Fluorescent ◽  
Protein Reduction

Imaging myosin 10 in cells

2004 ◽  
Vol 32 (5) ◽  
pp. 689-693 ◽  
Author(s):  
D. Tacon ◽  
P.J. Knight ◽  
M. Peckham
Keyword(s):  
Green Fluorescent Protein ◽  
Cell Biology ◽  
Fluorescent Protein ◽  
Major Task ◽  
Green Fluorescent ◽  
In Cells

Cellular motors (kinesin, dynein and myosin) are ubiquitous. A major task in cell biology is to determine how they function in cells. Here we focus on myosin 10, an intrafilopodial motor, and show how imaging green fluorescent protein fused to myosin 10 or its tail domains can help us understand the function of this myosin.

scholarly journals mCLCA4 ER processing and secretion requires luminal sorting motifs

2008 ◽  
Vol 295 (1) ◽  
pp. C279-C287 ◽  
Author(s):  
Chunlei Huan ◽  
Kai Su Greene ◽  
Bo Shui ◽  
Gwendolyn Spizz ◽  
Haitao Sun ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Green Fluorescent Protein ◽  
Enhanced Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Chloride Transport ◽  
Proteolytic Processing ◽  
Regulatory Sequences ◽  
Cellular Processing ◽  
Green Fluorescent

Ca+-activated Cl− channel (CLCA) proteins are encoded by a family of highly related and clustered genes in mammals that are markedly upregulated in inflammation and have been shown to affect chloride transport. Here we describe the cellular processing and regulatory sequences underlying murine (m) CLCA4 proteins. The 125-kDa mCLCA4 gene product is cleaved to 90- and 40-kDa fragments, and the NH2- and COOH-terminal fragments are secreted, where they are found in cell media and associated with the plasma membrane. The 125-kDa full-length protein is only found in the endoplasmic reticulum (ER), and specific luminal diarginine retention and dileucine forward trafficking signals contained within the CLCA4 sequence regulate export from the ER and proteolytic processing. Mutation of the dileucine luminal sequences resulted in ER trapping of the immaturely glycosylated 125-kDa peptide, indicating that proteolytic cleavage occurs following recognition of the trafficking motifs. Moreover, the mutated dileucine and diarginine signal sequences directed processing of a secreted form of enhanced green fluorescent protein in a manner consistent with the effects on mCLCA4.

scholarly journals Complexes between Herpes Simplex Virus Glycoproteins gD, gB, and gH Detected in Cells by Complementation of Split Enhanced Green Fluorescent Protein

2007 ◽  
Vol 81 (20) ◽  
pp. 11532-11537 ◽  
Author(s):  
Elisa Avitabile ◽  
Cristina Forghieri ◽  
Gabriella Campadelli-Fiume
Keyword(s):  
Herpes Simplex Virus ◽  
Green Fluorescent Protein ◽  
Herpes Simplex ◽  
Enhanced Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Split Egfp ◽  
Green Fluorescent ◽  
Simplex Virus ◽  
In Cells

ABSTRACT The interactions between herpes simplex virus gD and its nectin1 receptor or between gD, gB, and gH were analyzed by complementation of the N and C portions of split enhanced green fluorescent protein (EGFP) fused to the glycoproteins. The gDN-NectC complex was readily detected; the gDN-gCC complex was undetectable, highlighting the specificity of the assay. Split EGFP complementation was detected between proteins designated gDN+gHC, gDN+gBC, and gHN+gBC+wtgD (gB was deleted of endocytosis motifs), both in cells transfected with two-tree glycoproteins and in syncytia. The in situ assay provides evidence that gD interacts with gH and gB independently of each other and supports a model whereby gH and gB in complex exert their activities to gD.

scholarly journals Interaction of a Host Protein with Core Complexes of Bacteriophage Φ6 To Control Transcription

2010 ◽  
Vol 84 (9) ◽  
pp. 4821-4825 ◽  
Author(s):  
Xueying Qiao ◽  
Yang Sun ◽  
Jian Qiao ◽  
Leonard Mindich
Keyword(s):  
Green Fluorescent Protein ◽  
Rna Polymerase ◽  
Fluorescent Protein ◽  
Host Protein ◽  
Genomic Segment ◽  
Double Stranded Rna ◽  
Infection Period ◽  
The Family ◽  
Green Fluorescent ◽  
In Cells

ABSTRACT Bacteriophages of the family Cystoviridae have genomes consisting of three double-stranded RNA (dsRNA) segments, L, S, and M, packaged within a polyhedral capsid along with RNA polymerase. Transcription of genomic segment L is activated by the interaction of host protein YajQ with the capsid structure. Segment L codes for the proteins of the inner capsid, which are expressed early in infection. Green fluorescent protein (GFP) fusions with YajQ produce uniform fluorescence in uninfected cells and in cells infected with viruses not dependent on YajQ. Punctate fluorescence develops when cells are infected with YajQ-dependent viruses. It appears that the host protein binds to the infecting particles and remains with them during the entire infection period.

scholarly journals Green fluorescent protein-based monitoring of endoplasmic reticulum redox poise

2013 ◽  
Vol 4 ◽  
Author(s):  
Julia Birk ◽  
Thomas Ramming ◽  
Alex Odermatt ◽  
Christian Appenzeller-Herzog
Keyword(s):  
Endoplasmic Reticulum ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Redox Poise ◽  
Green Fluorescent
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