A novel mesoionic carbene based highly fluorescent Pd(ii) complex as an endoplasmic reticulum tracker in live cells

2018 ◽  
Vol 47 (44) ◽  
pp. 15646-15650 ◽  
Author(s):  
Sanjay K. Verma ◽  
Pratibha Kumari ◽  
Shagufi Naz Ansari ◽  
Mohd Ovais Ansari ◽  
Dondinath Deori ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Fluorescence Recovery After Photobleaching ◽  
Fluorescence Recovery ◽  
Live Cells

Synthesis of new organometallic MIC based mononuclear Pd(ii) complex 1, specifically target ER of live cells and have fluorescence recovery after photobleaching (FRAP) property.

scholarly journals Distinct Structural Requirements for Clustering and Immobilization of K+ Channels by PSD-95

1999 ◽  
Vol 113 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Nancy A. Burke ◽  
Koichi Takimoto ◽  
Danqing Li ◽  
Weiping Han ◽  
Simon C. Watkins ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Green Fluorescent Protein ◽  
Fluorescence Recovery After Photobleaching ◽  
Fluorescent Protein ◽  
Pdz Domain ◽  
Fluorescence Recovery ◽  
Live Cells ◽  
Structural Requirements ◽  
K Channels ◽  
Green Fluorescent

PDZ-domain–containing proteins such as PSD-95 have been implicated in the targeting and clustering of membrane proteins. Biochemical and immunohistochemical studies indicate that PSD-95 recognizes COOH-terminal S/TXV sequences present in Kv1 K+ channels. However, the effect of binding a PDZ domain on a target protein has not been studied in live cells. In the present study, a green fluorescent protein–Kv1.4 fusion protein is used to study the effect of PSD-95 on channel movement. Fluorescence recovery after photobleaching showed that PSD-95 can immobilize K+ channels in the plasma membrane in an all-or-none manner. Furthermore, time lapse imaging showed that channel clusters formed in the presence of PSD-95 are stable in size, shape, and position. As expected from previous reports, two green fluorescent protein–tagged COOH-terminal variants of Kv1.4, Δ15 and V655A, are not clustered by PSD-95. However, coexpression of PSD-95 with V655A, but not Δ15, leads to the appearance of PSD-95 immunoreactivity in the plasma membrane. Furthermore, fluorescence recovery after photobleaching studies show that V655A channels are immobilized by PSD-95. Thus, V655A channels can interact with PSD-95 in a manner that leads to channel immobilization, but not clustering. These experiments document for the first time that PSD-95 immobilizes target proteins. Additionally, the data presented here demonstrate that the structural requirements for protein clustering and immobilization by PSD-95 are distinct.

scholarly journals Improved Model of Fluorescence Recovery Expands the Application of Multiphoton Fluorescence Recovery after Photobleaching in Vivo

2009 ◽  
Vol 96 (12) ◽  
pp. 5082-5094 ◽  
Author(s):  
Kelley D. Sullivan ◽  
William H. Sipprell ◽  
Edward B. Brown ◽  
Edward B. Brown
Keyword(s):  
Fluorescence Recovery After Photobleaching ◽  
Fluorescence Recovery ◽  
Improved Model

scholarly journals Rotational dynamics of colloidal spheres probed with fluorescence recovery after photobleaching

2004 ◽  
Vol 120 (9) ◽  
pp. 4517-4529 ◽  
Author(s):  
M. P. Lettinga ◽  
G. H. Koenderink ◽  
B. W. M. Kuipers ◽  
E. Bessels ◽  
A. P. Philipse
Keyword(s):  
Fluorescence Recovery After Photobleaching ◽  
Rotational Dynamics ◽  
Fluorescence Recovery ◽  
Colloidal Spheres

scholarly journals Role for Actin in the Polarized Release of Rotavirus

2007 ◽  
Vol 81 (9) ◽  
pp. 4892-4894 ◽  
Author(s):  
Agnès Gardet ◽  
Michelyne Breton ◽  
Germain Trugnan ◽  
Serge Chwetzoff
Keyword(s):  
Fluorescence Recovery After Photobleaching ◽  
Spike Protein ◽  
Fluorescence Recovery ◽  
Actin Network ◽  
Apical Pole ◽  
Apical Side ◽  
Functional Consequences ◽  
Diffusional Mobility

ABSTRACT Rotaviruses are characterized by polarized release from the apical side of infected enterocytes, and the rotavirus VP4 spike protein specifically binds to the actin network at the apical pole of differentiated enterocytic cells. To determine the functional consequences of this VP4-actin interaction, fluorescence recovery after photobleaching experiments were carried out to measure the diffusional mobility of VP4 associated with the microfilaments. Results show that VP4 binds to barbed ends of microfilaments by using actin treadmilling. Actin treadmilling inhibition results in the loss of rotavirus apical preferential release, suggesting a major role for actin in polarized rotavirus release.

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