Protein tyrosine kinases schematic diagram

Figure 1. Schematic diagram of protein phosphatases and protein kinases (PK) on opening or closure of connexons. PTK protein tyrosine kinase MAPK mitogen activated protein kinases CasK casein kinase P indicates phosphorylation.

FIGURE 1 2-2 Schematic diagram of the phosphorylation sites on each of the four 60kDa subunits of tyrosine hydroxylase (TOHase). Serine residues at the N-terminus of each of the four subunits of TOHase can be phosphorylated by at least five protein kinases. (J), Calcium/calmodulin-dependent protein kinase II (CaM KII) phosphorylates serine residue 19 and to a lesser extent serine 40. (2), cAMP-dependent protein kinase (PKA) phosphorylates serine residue 40. (3), Calcium/phosphatidylserine-activated protein kinase (PKC) phosphorylates serine 40. (4), Extracellular receptor-activated protein kinase (ERK) phosphorylates serine 31. (5), A cdc-like protein kinase phosphorylates serine 8. Phosphorylation on either serine 19 or 40 increases the activity of TOHase. Serine 19 phosphorylation requires the presence of an activator protein , also known as 14-3-3 protein, for the expression of increased activity. Phosphorylation of serines 8 and 31 has little effect on catalytic activity. The model shown includes the activation of ERK by an ERK kinase. The ERK kinase is activated by phosphorylation by PKC. (With permission from reference [72].)... 

FIGURE 23-5 Schematic diagram of tyrosine hydroxylase with sites of phosphorylation indicated (yellow) along with the protein kinases. 

Fig. 11.4 Schematic diagram ofthe 11-2 receptor complex. The II-2R is composed of three subunits, IL-2Ra, IL-2R/7 yc. The Box 1 and Box 2 domains are conserved among members ofthe cytokine receptor superfamily, and a variable spacer region V intervenes Boxl and Box2. The Boxl-V-Box2 regions encompass the sites of association with the Janus kinases (Jak). Jakl associates constitutively with IL-2R/> and Jak3 associates constitutively with yc. Both IL-2R/> and yc encode multiple cytoplasmic tyrosine residues with approximated locations shown. At least some of these tyrosines on both chains become phosphorylated following receptor activation whereupon they serve to recruit effector proteins to direct downstream signaling events.

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