![]() 1999), and substrate selection is thought to be regulated in vivo via subcellular localization and docking sites in specific substrates. The family members appear to have similar substrate specificity in vitro ( Pulgar et al. Drosophila has eight CKI family members, and Caenorhabditis elegans has 87 ( Plowman et al. In vivo phosphatases keep it constitutively active in many cases ( Rivers et al. The long C-terminal extensions ofĬKIδ and CKIϵ, however, are autophosphorylated, and this phosphorylation inhibits the activity of the kinase domain, although In general, kinases in the family are constitutively active. Kinase domains, the CKIγ isoforms are ∼50% identical in their C-terminal tails, and the long C-terminal extensions of CKIδĪnd CKIϵ have ∼53% identity. CKIα and CKIβ are 76% identical outside their In the length and amino acid sequence of their N- and C-terminal extensions. Outside of the kinase domain, CKI family members fall into subfamilies that have little homology to each other and differ Kinases by the presence of the sequence S-I-N instead of A-P-E in kinase domain VIII ( Hanks and Hunter 1995). The family members have the highest homology in their kinase domains (53%–98% identical) and differ from most other protein Have seven family members (sometimes referred to as isoforms, but encoded by distinct genes): α, β, γ1, γ2, γ3, δ, and ϵ. The CKI family of monomeric serine–threonine protein kinases is found in eukaryotic organisms from yeast to human. Work in the last 7 years has shown a role for multiple CKI family members in both positively and negatively regulating Of membrane transport, cell division, DNA repair, circadian rhythms, and nuclear localization (for review, see Gross and Anderson 1998 Knippschild et al. The CKI family of serine/threonine protein kinases is involved in many diverse and important cellular functions, such as regulation Previous Section Next Section Introduction to casein kinase I (CKI) ![]()
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