Negative Regulation of LRP6 Function by Casein Kinase I ϵ Phosphorylation
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چکیده
منابع مشابه
Regulation of casein kinase 2 by phosphorylation/dephosphorylation.
The effects of various polycation-stimulated (PCS) phosphatases and of the active catalytic subunit of the ATPMg-dependent (AMDc) protein phosphatase on the activity of casein kinase 2 (CK-2) were investigated by using the synthetic peptide substrate Ser-Glu-Glu-Glu-Glu-Glu, whose phosphorylated derivative is entirely insensitive to these protein phosphatases. Previous dephosphorylation of nati...
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Calcineurin is a Ca2+/calmodulin-regulated protein phosphatase required for Saccharomyces cerevisiae to respond to a variety of environmental stresses. Calcineurin promotes cell survival during stress by dephosphorylating and activating the Zn-finger transcription factor Crz1p/Tcn1p. Using a high-throughput assay, we screened 119 yeast kinases for their ability to phosphorylate Crz1p in vitro a...
متن کاملRegulation of Casein Kinase I Activity by Wnt Signaling*
The Wnt/ -catenin signaling pathway is important in both development and cancer. Casein kinase I (CKI ) is a positive regulator of the canonical Wnt pathway. CKI itself can be regulated in vitro by inhibitory autophosphorylation, and recent data suggest that in vivo kinase activity can be regulated by extracellular stimuli. We show here that the phosphorylation state and kinase activity of CKI ...
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Alzheimer’s disease (AD) is associated with accumulation of the neurotoxic peptide amyloid(A ), which is produced by sequential cleavage of amyloid precursor protein (APP) by the aspartyl protease -secretase and the presenilin-dependent protease -secretase. An increase of casein kinase 1 (CK1) expression has been described in the human AD brain. We show, by using in silico analysis, that APP, -...
متن کاملPhosphorylation of fibrinogen by casein kinase 1.
Casein kinase 1 phosphorylated human fibrinogen, in a reaction that did not use GTP as phosphoryl donor and was neither stimulated by cyclic AMP or Ca2+, nor inhibited by the cyclic AMP-dependent protein kinase inhibitor protein. Maximal incorporation averaged 4 mol of phosphate per mol of fibrinogen, most of it in the largest CNBr-fragment of the alpha-chain. Phosphoamino acid analysis reveale...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2006
ISSN: 0021-9258
DOI: 10.1074/jbc.m510580200