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A synthetic β-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase [PDF]
FEBS Letters, 1991 The phosphopeptide Ser (P)‐Ser(P)‐Ser‐(P)‐Glu‐Glu‐Ser11‐Ilc‐Thr, reproducing the 17‐24 segment of β‐casein Λ1 including the seryl residue (Ser‐22) which is targeted by casein kinase‐1 was synthesized and used as model substrate for this enzyme. Its phosphorylation efficiency is actually higher than that of intact β‐casein (similar Vmax and 14 μM vs 50
Flavio Meggio +2 more
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Casein kinase 1: Complexity in the family
The International Journal of Biochemistry & Cell Biology, 2011The CK1 family of serine/threonine kinases regulates diverse cellular processes, through binding to and phosphorylation a myriad of protein substrates. CK1 prefers substrates primed by prior phosphorylation, and works closely with other kinases in the Wnt pathway. CK1 is itself regulated by posttranslational modification, including autophosphorylation.
Cheong, J.K., Virshup, D.M.
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Phosphorylation of calcineurin by glycogen synthase (casein) kinase-1
Biochemistry and Cell Biology, 1987A previous study demonstrated that calcineurin preparations contain variable amounts of endogenous phosphate. This observation suggests that calcineurin may be regulated by protein phosphorylation. In this study we have used calcineurin as a potential substrate for eight different protein kinases and significant phosphorylation was observed only with ...
T J, Singh, J H, Wang
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Archives of Biochemistry and Biophysics, 1986
Casein kinase 1 phosphorylated rabbit skeletal muscle glycogen synthase at both seryl and threonyl residues. With glycogen synthase phosphorylated up to 7.5 mol phosphate/mol subunit, about 26% of the phosphate was present in the N-terminal cyanogen bromide fragment (CB1) and 74% in the C-terminal fragment (CB2).
M D, Guasch +3 more
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Casein kinase 1 phosphorylated rabbit skeletal muscle glycogen synthase at both seryl and threonyl residues. With glycogen synthase phosphorylated up to 7.5 mol phosphate/mol subunit, about 26% of the phosphate was present in the N-terminal cyanogen bromide fragment (CB1) and 74% in the C-terminal fragment (CB2).
M D, Guasch +3 more
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Role for casein kinase 2 in the regulation of HIF‐1 activity
International Journal of Cancer, 2005AbstractHypoxia‐inducible factor‐1 (HIF‐1) is a heterodimeric transcription factor that plays a major role in cellular adaptation to hypoxia. The mechanisms regulating HIF‐1 activity occurs at multiple levels in vivo. The HIF‐1α subunit is highly sensible to oxygen and is rapidly degraded by the proteasome 26S in normoxia.
Mottet, Denis +4 more
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Casein kinase 1 and Wnt/β-catenin signaling
Current Opinion in Cell Biology, 2014Casein kinase 1 (CK1) members play a critical and evolutionary conserved role in Wnt/β-catenin signaling. They phosphorylate several pathway components and exert a dual function, acting as both Wnt activators and Wnt inhibitors. Recent discoveries suggest that CK1 members act in a coordinated manner to regulate early responses to Wnt and notably that ...
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Identification of casein kinase-1 phosphorylation sites on TDP-43
Biochemical and Biophysical Research Communications, 2009TAR DNA-binding protein of 43 kDa (TDP-43) is deposited as hyperphosphorylated cytoplasmic and intranuclear inclusions in brains of patients with frontotemporal lobar degeneration with ubiquitinated inclusions and amyotrophic lateral sclerosis. In this study, we identified 29 phosphorylation sites on recombinant TDP-43 that are phosphorylated by casein
Fuyuki, Kametani +6 more
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Inhibition of glycogen synthase (casein) kinase-1 by heparin
Archives of Biochemistry and Biophysics, 1988Previous reports have shown that heparin is an inhibitor of casein kinase-2 (CK-2). It is unclear whether heparin is also an inhibitor of glycogen synthase (casein) kinase-1 (CK-1), a type 1 casein kinase. In this study it is shown that CK-1 is potently inhibited by heparin when phosvitin or calcineurin are used as substrates.
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Modulators of rat liver cytosol casein kinases 1 and 2
Biochemical and Biophysical Research Communications, 1982Abstract Rat liver cytosol casein kinases 1 and 2 are similarly activated by spermine and inhibited by caffeine. On the contrary they are differently affected by heparin and basic proteins. Low concentrations of heparin inhibited selectively the phosphorylation of casein by casein kinase 2 whereas protamine and histones inhibited specifically casein ...
M, Plana, M D, Guasch, E, Itarte
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Inhibition of Casein Kinase 1 Alpha in Acute Myeloid Leukemia
New England Journal of Medicine, 2018Suppression of Casein Kinase 1 Alpha in AML Casein kinase 1 alpha targets the apoptosis-inducing protein P53 for degradation, and a paucity of functional P53 underlies the neoplastic behavior of ca...
Benjamin L, Ebert, Jan, Krönke
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