scholarly journals Chapter 15 Characterization of Chemokine Receptor CXCR2 Interacting Proteins Using a Proteomics Approach to Define the CXCR2 “Chemosynapse”

Author(s):  
Dayanidhi Raman ◽  
Nicole F. Neel ◽  
Jiqing Sai ◽  
Raymond L. Mernaugh ◽  
Amy-Joan L. Ham ◽  
...  
2012 ◽  
Vol 11 (11) ◽  
pp. 1263-1273 ◽  
Author(s):  
Pavlos Fanis ◽  
Nynke Gillemans ◽  
Ali Aghajanirefah ◽  
Farzin Pourfarzad ◽  
Jeroen Demmers ◽  
...  

Chromatin target of Prmt1 (Chtop) is a vertebrate-specific chromatin-bound protein that plays an important role in transcriptional regulation. As its mechanism of action remains unclear, we identified Chtop-interacting proteins using a biotinylation-proteomics approach. Here we describe the identification and initial characterization of Five Friends of Methylated Chtop (5FMC). 5FMC is a nuclear complex that can only be recruited by Chtop when the latter is arginine-methylated by Prmt1. It consists of the co-activator Pelp1, the Sumo-specific protease Senp3, Wdr18, Tex10, and Las1L. Pelp1 functions as the core of 5FMC, as the other components become unstable in the absence of Pelp1. We show that recruitment of 5FMC to Zbp-89, a zinc-finger transcription factor, affects its sumoylation status and transactivation potential. Collectively, our data provide a mechanistic link between arginine methylation and (de)sumoylation in the control of transcriptional activity.


Cytokine ◽  
2005 ◽  
Vol 31 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Wenxian Fu ◽  
Yu Zhang ◽  
Jun Zhang ◽  
Wei-Feng Chen

BMC Cancer ◽  
2014 ◽  
Vol 14 (1) ◽  
Author(s):  
Anastasios Stofas ◽  
Georgia Levidou ◽  
Christina Piperi ◽  
Christos Adamopoulos ◽  
Georgia Dalagiorgou ◽  
...  

2015 ◽  
Vol 87 (4) ◽  
pp. 639-648 ◽  
Author(s):  
Danny J. Scholten ◽  
Maikel Wijtmans ◽  
Jeffrey R. van Senten ◽  
Hans Custers ◽  
Ailas Stunnenberg ◽  
...  

2021 ◽  
Author(s):  
Alejandro Saettone Chipana

The thesis aims to identify and initiate functional characterization of the SWI/SNF and ISWI complexes in Tetrahymena thermophila. Through affinity purification of the conserved subunit Snf5 followed by mass spectrometry (AP-MS), I identified the first SWI/SNF complex in protists. One of the subunits I found is a small bromodomain containing protein named Ibd1. Through AP-MS of Ibd1 I found Ibd1 is versatile and interacts with several additional chromatin remodeling complexes. Bromodomains are known to have affinity for acetylated lysine residues within proteins such as histones. A peptide array experiment suggests that Ibd1 also has affinity for acetylated chromatin. Indirect immunofluorescence (IF) of Ibd1 hints at a role in transcription. My analysis of Tetrahymena Iswi1 shows expression during meiosis, vegetative growth and starvation. IF data shows its localization is consistent with Iswi1 function in mitosis/meiosis or maintenance of silent chromatin. AP-MS of ISW1 discovered several interacting proteins of unknown function.


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