Cross-talk between Lysine-Modifying Enzymes Controls Site-Specific DNA Amplifications

Cross-Talk between Shp1 and PIPKIg Controls Leukocyte Recruitment

Cross-Talk between Shp1 and PIPKIγ Controls Leukocyte Recruitment.

Neutrophil recruitment to the site of inflammation plays a pivotal role in host defense. However, overwhelming activation and accumulation of neutrophils in the tissue may cause tissue damage and autoimmunity due to the release of cytokines, oxidants, and proteases. Neutrophil adhesion in acute inflammation is initiated by activation of αLβ2 (LFA-1), which can be induced by rolling on E-selecti...

Cross talk between DNA repair and chromatin modifications

Myh1 is a DNA glycosylase that is involved in base excision repair after oxidation damage. It excises mis-incorporated adenine opposite to the lesion 8-oxoG. The human homolog MUTYH, is important in tumour development as mutations in the MUTYH lead to G: C to T: A transversion mutations in MUTYH hereditary colon cancer. Pst2 (Sin3 homolog) is a scaffold protein and forms a complex with Clr6 His...

Interplay between chromatin-modifying enzymes controls colon cancer progression through Wnt signaling.

Cancer progression is associated with epigenetic alterations, such as changes in DNA methylation, histone modifications or variants incorporation. The p400 ATPase, which can incorporate the H2A.Z variant, and the Tip60 histone acetyltransferase are interacting chromatin-modifying proteins crucial for the control of cell proliferation. We demonstrate here that Tip60 acts as a tumor suppressor in...

Site-Specific Reactivity of Nonenzymatic Lysine Acetylation

Protein acetylation of lysine ε-amino groups is abundant in cells, particularly within mitochondria. The contribution of enzyme-catalyzed and nonenzymatic acetylation in mitochondria remains unresolved. Here, we utilize a newly developed approach to measure site-specific, nonenzymatic acetylation rates for 90 sites in eight native purified proteins. Lysine reactivity (as second-order rate const...