High impact information on CSNK1A1

• The CKI PCR product was used to probe a bovine brain cDNA library from which cDNAs corresponding to CKI (CKI-alpha) and two homologous enzymes (CKI-beta and CKI-gamma) were identified [1].
• From these biochemical and immunological criteria it is concluded that the 82-kDa protein is the human neutrophil homolog of MARCKS, the myristoylated, alanine-rich C kinase substrate previously described in bovine and rat brain and in murine fibroblasts and macrophages [2].
• These findings strongly suggest that C-kinase plays an important role in mediating tracheal smooth muscle contraction [3].
• In addition, BAY K 8644 (20 nM), which has a minimal effect on tension by itself, could significantly enhance contraction induced by C-kinase activators [3].
• In contrast, ionophores and C-kinase activators, in combination, acted synergistically to produce a prompt and sustained contractile response that is reminiscent of that observed in response to carbachol, a cholinergic agonist [3].

Biological context of CSNK1A1

• We evaluated the protein kinase C phosphorylation sites in a major cellular substrate for the kinase, a protein of apparent Mr 80,000 in bovine and 60,000 in chicken tissues; we have recently determined the primary sequences of these proteins and tentatively named them the myristoylated alanine-rich C kinase substrates [4].
• Besides casein, CPK phosphorylates in vitro the catalytic subunit of bovine brain calcineurin (CaN), a typical substrate of type 1 mammalian casein kinase (CK-1) in vitro [5].
• Since C-kinase plays an important role in the signal transduction leading to the cell proliferation and K252a inhibits C-kinase in vitro, the antiproliferative effect of K252a to carotid smooth muscle cells is likely to be exerted through c-kinase dependent pathway [6].

Anatomical context of CSNK1A1

• These data imply that the initial transient rise in the [Ca2+] of the cell cytosol plays a role in determining the extent to which C-kinase is shifted from its calcium-insensitive to its calcium-sensitive form [7].
• Adrenal glomerulosa cells were shown to contain the calcium-activated, phospholipid-dependent protein kinase (C-kinase) [8].
• Myristoylated alanine-rich C kinase substrates (MARCKS) is a prominent protein kinase C (PKC) substrate that is targeted to the plasma membrane by an aminoterminal myristoyl group [9].
• A calcium phospholipid-dependent protein kinase (C-kinase) activity was detected in the soluble fraction of rod outer segments (ROS) of the bovine retina [10].
• These results suggest that calcium, phospholipids and the C-kinase enzyme may play an important role in the functional regulation of rod photoreceptors and, with retinal, perhaps in the visual process as well [10].

Associations of CSNK1A1 with chemical compounds

• The effects of divalent ionophores (A23187 and ionomycin), Ca2+ channel agonist (BAY K 8644), and protein kinase C (C-kinase) activators [phorbol 12-myristate 13-acetate (PMA), mezerein] on bovine tracheal smooth muscle contraction were investigated [3].
• The present studies were undertaken to determine the respective roles of the two angiotensin II-induced changes in cellular calcium metabolism in modulating events during the sustained phase of cellular response which is thought to be mediated by the C-kinase branch of the calcium messenger system [7].
• This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase [11].
• CK-3 (Mr 32,000) is readily separated from CK-2 by gel filtration and from CK-1 by hydroxyapatite chromatography [12].
• The inhibition of CK-1 by heparin can be reversed by KCl (greater than 100 mM) [13].

Other interactions of CSNK1A1

• Prephosphorylation of tau by A-kinase, C-kinase, or CK-2 (but not by CK-1, CaM kinase II or Gr kinase) increased both the rate and extent of a subsequent phosphorylation catalyzed by GSK-3 by several-fold [14].
• Both GL and glycyrrhetinic acid (GA) at 100 microM significantly inhibited RNase activities of these two gbPs, both of which functioned as phosphate acceptors of C-kinase in vitro [15].

References