Cell Signaling part 2
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1 15 Cell Signaling part 2
2 Functions of Cell Surface Receptors Other cell surface receptors are directly linked to intracellular enzymes. The largest family of these is the receptor protein tyrosine kinases, which phosphorylate their substrates on tyrosine residues. Examples: receptors for EGF, NGF, PDGF, insulin, and other growth factors.
3 Functions of Cell Surface Receptors All have an N-terminal extracellular ligandbinding domain, a single transmembrane α helix, and a cytosolic C-terminal domain with protein-tyrosine kinase activity.
4 Functions of Cell Surface Receptors Binding of ligands to the extracellular domains activates their cytosolic kinase domains. This results in phosphorylation of both the receptors and intracellular target proteins that propagate the signal. The first step is ligand-induced receptor dimerization. This results in receptor autophosphorylation, as the two polypeptide chains cross-phosphorylate each other.
5 Figure Dimerization and autophosphorylation of receptor protein-tyrosine kinases
6 Functions of Cell Surface Receptors Autophosphorylation has two roles: Phosphorylation of tyrosine in the catalytic domain increases protein kinase activity. Phosphorylation of tyrosine outside the catalytic domain creates binding sites for other proteins that transmit signals downstream from the activated receptors.
7 Functions of Cell Surface Receptors The downstream signaling molecules have domains that bind to specific phosphotyrosinecontaining peptides. Example: SH2 domains
8 Functions of Cell Surface Receptors Cytokine receptors function in association with nonreceptor protein-tyrosine kinases. Ligand binding induces dimerization of receptors, and cross-phosphorylation of associated nonreceptor protein-tyrosine kinases. The activated kinases then phosphorylate the receptor. This provides phosphotyrosine-binding sites for recruitment of downstream signaling molecules with SH2 domains.
9 Figure Signaling from cytokine receptors
10 Functions of Cell Surface Receptors Some enzyme-linked receptors are associated with other enzymatic activities: Protein-tyrosine phosphatases remove phosphate groups from phosphotyrosine, counterbalancing the effects of protein-tyrosine kinases. Protein-serine/ threonine kinase; Transforming growth factor β (TGF- β) receptors Receptor guanylyl cyclases have a cytosolic domain that catalyzes formation of cyclic GMP.
11 Intracellular signal transduction: Intracellular signaling was first studied in epinephrine, which signals the breakdown of glycogen to glucose. The epinephrine receptor is coupled to adenylyl cyclase via a G protein that stimulates enzymatic activity, increasing the concentration of cyclic AMP (camp), a second messenger. camp is formed from ATP by adenylyl cyclase and degraded to AMP by camp phosphodiesterase.
12 Figure Synthesis and degradation of camp
13 camp effects are mediated by camp-dependent protein kinase, or protein kinase A. Inactive form has two regulatory and two catalytic subunits. camp binds to the regulatory subunits, which dissociate. The free catalytic subunits can then phosphorylate serine on target proteins.
14 In glycogen metabolism, protein kinase A phosphorylates two enzymes: Phosphorylase kinase is activated, and in turn activates glycogen phosphorylase. Glycogen synthase is inactivated. So, glycogen breakdown is stimulated and glycogen synthesis is blocked.
15 Figure Regulation of glycogen metabolism by protein kinase A
16 Signal amplification: each molecule of epinephrine activates one receptor. Each receptor may activate up to 100 molecules of G s, which then stimulates adenylyl cyclase. This catalyzes synthesis of many camp. Each molecule of protein kinase A phosphorylates many molecules of phosphorylase kinase, and so forth.
17 camp can activate transcription of genes with the camp response element, or CRE regulatory sequence. The free catalytic subunit of protein kinase A goes to the nucleus and phosphorylates the transcription factor CREB (CRE-binding protein). This leads to expression of camp-inducible genes.
18 Protein phosphorylation is rapidly reversed by protein phosphatases, which terminates responses initiated by receptor activation of protein kinases.
19 camp can also directly regulate ion channels: camp opens Na + channels in the plasma membrane, leading to initiation of a nerve impulse. cgmp is also an important second messenger. cgmp is formed from GTP by guanylyl cyclases and degraded to GMP by a phosphodiesterase. cgmp mediates biological responses, such as blood vessel dilation.
20 Hydrolysis of membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP 2 ) by phospholipase C produces two second messengers: Diacylglycerol (DAG) Inositol 1,4,5-trisphosphate (IP 3 )
21 PLC-γ has SH2 domains that associate with receptor protein tyrosine kinases and tyrosine phosphorylation increases PLC-γ activity, stimulating hydrolysis of PIP 2.
22 DAG remains associated with the plasma membrane and activates proteinserine/threonine kinases of the protein kinase C family. IP 3 is released to the cytosol, where it signals release of Ca 2+ from the ER.
23 One of the major Ca 2+ -binding proteins is calmodulin. Ca 2+ /calmodulin then binds to target proteins, including protein kinases.
24 Ca 2+ is also increased by uptake of extracellular Ca 2+ by regulated channels in the plasma membrane. In electrically excitable cells of nerve and muscle, voltage-gated Ca 2+ channels are opened by membrane depolarization. The resulting increase in intracellular Ca 2+ signals further release of Ca 2+ from the ER by opening Ca 2+ channels (ryanodine receptors) in the ER membrane.
25 Figure Regulation of intracellular Ca 2+ in electrically excitable cells
26 The MAP kinase pathway is a cascade of protein kinases that is highly conserved in evolution, found in all eukaryotic cells. MAP kinases (mitogen-activated protein kinases) are protein-serine/threonine kinases. MAP kinases initially found in mammalian cells belong to the ERK (extracellular signal-regulated kinase) family. Activation of ERK is mediated by two upstream protein kinases that are coupled to growth factor receptors by the Ras GTP-binding protein.
27 Activation of Ras leads to activation of protein serine/threonine kinase. Raf This phosphorylates and activates a second protein kinase, MEK (MAP kinase/erk kinase).
28 Ras is activated by guanine nucleotide exchange factors that stimulate exchange of GDP for GTP. Ras-GTP activity is terminated by GTP hydrolysis, stimulated by interaction of Ras- GTP with GTPaseactivating proteins (GAPs).
29 Mutations of ras genes in human cancers inhibit GTP hydrolysis by Ras proteins. The mutated Ras proteins therefore remain continuously in the active GTP-bound form, driving the proliferation of cancer cells even in the absence of growth factor stimulation.
30 One mode of Ras activation is mediated by receptor protein-tyrosine kinases. Autophosphorylation of these receptors results in association with Ras guanine nucleotide exchange factors (e.g., Sos) as a result of SH2- mediated protein interactions.
31 Active Ras binds with Raf protein-serine/threonine kinase. Raf initiates a protein kinase cascade, leading to ERK activation. Activated ERK goes to the nucleus, where it regulates transcription factors by phosphorylation.
32 Figure Pathways of MAP kinase activation in mammalian cells
33 Specificity of MAP kinase signaling is maintained partly by physical association on scaffold proteins. Example: KSR scaffold protein organizes ERK and its upstream activators Raf and MEK into a signaling cassette.
34 Figure The JAK/STAT pathway Figure Signaling from TGF- receptors
35 Figure NF- B signaling from the TNF receptor
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