A luminescent lanthanide approach towards direct visualization of primary cilia in living cells

2017 ◽  
Vol 53 (52) ◽  
pp. 7084-7087 ◽  
Author(s):  
Hongguang Li ◽  
Rongfeng Lan ◽  
Chi-Fai Chan ◽  
Guochen Bao ◽  
Chen Xie ◽  
...  

A simple and direct imaging tool (HGEu001) for primary cilia based on long-lived europium luminescence is firstly presented.

2016 ◽  
Vol 52 (25) ◽  
pp. 4636-4639 ◽  
Author(s):  
Fei Liu ◽  
Juan Du ◽  
Da Song ◽  
Meiying Xu ◽  
Guoping Sun

MPT-Cy2exhibited excellent selectivity and sensitivity toward ˙OH over other ROS and showed a high potential for the imaging of endogenous ˙OH in living cells and various types of bacteria.


2020 ◽  
Author(s):  
Avishek Prasai ◽  
Marketa Schmidt Cernohorska ◽  
Klara Ruppova ◽  
Veronika Niederlova ◽  
Monika Andelova ◽  
...  

AbstractBardet-Biedl Syndrome (BBS) is a pleiotropic ciliopathy caused by dysfunction of primary cilia. Most BBS patients carry mutations in one of eight genes encoding for subunits of a protein complex, BBSome, which mediates the trafficking of ciliary cargoes. Although, the structure of the BBSome has been resolved recently, the mechanism of assembly of this complicated complex in living cells is poorly understood. We generated a large library of human retinal epithelial cell lines deficient in particular BBSome subunit and expressing another subunit tagged with a fluorescent protein. We performed a comprehensive analysis of these cell lines using biochemical and microscopy approaches. Our data revealed that the BBSome formation is a sequential process including a step of the pre-BBSome assembly at pericentriolar satellites nucleated by BBS4, followed by the translocation of the BBSome into the ciliary base mediated by BBS1.


Nanoscale ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 6144-6152
Author(s):  
Melonie P. Thomas ◽  
Namal Wanninayake ◽  
Manisha De Alwis Goonatilleke ◽  
Doo Young Kim ◽  
Beth S. Guiton

Direct visualization of dopant atom configuration in carbon nano-onions provides structure–property link to catalytic activity.


2008 ◽  
Vol 229 (1) ◽  
pp. 67-77 ◽  
Author(s):  
C. WANG ◽  
G. FU ◽  
J. WANG ◽  
G. WANG ◽  
Y. CHENG ◽  
...  

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Haitham A. Shaban ◽  
Roman Barth ◽  
Kerstin Bystricky

AbstractThe eukaryotic genome is hierarchically structured yet highly dynamic. Regulating transcription in this environment demands a high level of coordination to permit many proteins to interact with chromatin fiber at appropriate sites in a timely manner. We describe how recent advances in quantitative imaging techniques overcome caveats of sequencing-based methods (Hi-C and related) by enabling direct visualization of transcription factors and chromatin at high resolution, from single genes to the whole nucleus. We discuss the contribution of fluorescence imaging to deciphering the principles underlying this coordination within the crowded nuclear space in living cells and discuss challenges ahead.


2018 ◽  
Author(s):  
Shi-Rong Hong ◽  
Cuei-Ling Wang ◽  
Yao-Shen Huang ◽  
Yu-Chen Chang ◽  
Ya-Chu Chang ◽  
...  

AbstractTubulin post-translational modifications (PTMs) occur spatiotemporally throughout cells and are suggested to be involved in a wide range of cellular activities. However, the complexity and dynamic distribution of tubulin PTMs within cells have hindered the understanding of their physiological roles in specific subcellular compartments. Here we develop a method to rapidly deplete tubulin glutamlyation inside the primary cilia, a microtubule-based sensory organelle protruding on the cell surface, by targeting an engineered deglutamylase to the cilia in minutes. This rapid deglutamylation quickly leads to altered ciliary functions such as kinesin-2-mediated anterograde intraflagellar transport and Hedgehog signaling, along with no apparent crosstalk to other PTMs such as acetylation and detyrosination. Our study offers a feasible approach to spatiotemporally manipulate tubulin PTMs in living cells. Future expansion of the repertoire of actuators that regulate PTMs may facilitate a comprehensive understanding of how diverse tubulin PTMs encode ciliary as well as cellular functions.


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