Analysis of the cGMP/cAMP Interactome Using a Chemical Proteomics Approach in Mammalian Heart Tissue Validates Sphingosine Kinase Type 1-interacting Protein as a Genuine and Highly Abundant AKAP

2006 ◽  
Vol 5 (6) ◽  
pp. 1435-1447 ◽  
Author(s):  
Arjen Scholten ◽  
Mee Kian Poh ◽  
Toon A. B. van Veen ◽  
Bas van Breukelen ◽  
Marc A. Vos ◽  
...  
Keyword(s):  
Sphingosine Kinase ◽  
Heart Tissue ◽  
Interacting Protein ◽  
Chemical Proteomics ◽  
Mammalian Heart ◽  
Proteomics Approach

scholarly journals Human Immunodeficiency Virus Type 1 Replication and Regulation of APOBEC3G by Peptidyl Prolyl Isomerase Pin1

2008 ◽  
Vol 82 (20) ◽  
pp. 9928-9936 ◽  
Author(s):  
Koichi Watashi ◽  
Mohammad Khan ◽  
Venkat R. K. Yedavalli ◽  
Man Lung Yeung ◽  
Klaus Strebel ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Cytidine Deaminase ◽  
Prolyl Isomerase ◽  
Interacting Protein ◽  
New Findings ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT APOBEC3G (A3G) is a cytidine deaminase that restricts human immunodeficiency virus type 1 (HIV-1) replication. HIV-1 synthesizes a viral infectivity factor (Vif) to counter A3G restriction. Currently, it is poorly understood how A3G expression/activity is regulated by cellular factors. Here, we show that the prolyl isomerase Pin1 protein modulates A3G expression. Pin1 was found to be an A3G-interacting protein that reduces A3G expression and its incorporation into HIV-1 virion, thereby limiting A3G-mediated restriction of HIV-1. Intriguingly, HIV-1 infection modulates the phosphorylation state of Pin1, enhancing its ability to moderate A3G activity. These new findings suggest a potential Vif-independent way for HIV-1 to moderate the cellular action of A3G.

A Quantitative Chemical Proteomics Approach for Site-specific Stoichiometry Analysis of Ubiquitination

2018 ◽  
Vol 58 (2) ◽  
pp. 537-541 ◽  
Author(s):  
Yunan Li ◽  
Jonathan Evers ◽  
Ang Luo ◽  
Luke Erber ◽  
Zachary Postler ◽  
...  
Keyword(s):  
Chemical Proteomics ◽  
Site Specific ◽  
Proteomics Approach ◽  
Quantitative Chemical

scholarly journals A Chemical Proteomics Approach to Profiling the ATP-binding Proteome ofMycobacterium tuberculosis

2013 ◽  
Vol 12 (6) ◽  
pp. 1644-1660 ◽  
Author(s):  
Lisa M. Wolfe ◽  
Usha Veeraraghavan ◽  
Susan Idicula-Thomas ◽  
Stephan Schürer ◽  
Krister Wennerberg ◽  
...  
Keyword(s):  
Atp Binding ◽  
Chemical Proteomics ◽  
Ofmycobacterium Tuberculosis ◽  
Proteomics Approach

scholarly journals Early Activation of Sphingosine Kinase in Mast Cells and Recruitment to FcεRI Are Mediated by Its Interaction with Lyn Kinase

2004 ◽  
Vol 24 (19) ◽  
pp. 8765-8777 ◽  
Author(s):  
Nicole Urtz ◽  
Ana Olivera ◽  
Elisa Bofill-Cardona ◽  
Robert Csonga ◽  
Andreas Billich ◽  
...  
Keyword(s):  
Mast Cells ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Immunoglobulin E ◽  
Sphingosine Kinase ◽  
Lipid Kinase ◽  
Lyn Kinase ◽  
Sphingosine 1 Phosphate ◽  
High Affinity Receptor

ABSTRACT Sphingosine kinase has been recognized as an essential signaling molecule that mediates the intracellular conversion of sphingosine to sphingosine-1-phosphate. In mast cells, induction of sphingosine kinase and generation of sphingosine-1-phosphate have been linked to the initial rise in Ca2+, released from internal stores, and to degranulation. These events either precede or are concomitant with the activation of phospholipase C-γ and the generation of inositol trisphosphate. Here we show that sphingosine kinase type 1 (SPHK1) interacts directly with the tyrosine kinase Lyn and that this interaction leads to the recruitment of this lipid kinase to the high-affinity receptor for immunoglobulin E (FcεRI). The interaction of SPHK1 with Lyn caused enhanced lipid and tyrosine kinase activity. After FcεRI triggering, enhanced sphingosine kinase activity was associated with FcεRI in sphingolipid-enriched rafts of mast cells. Bone marrow-derived mast cells from Lyn−/ − mice, compared to syngeneic wild-type cells, were defective in the initial induction of SPHK1 activity, and the defect was overcome by retroviral Lyn expression. These findings position the activation of SPHK1 as an FcεRI proximal event.

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