Signal Transduction I

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1 Signal Transduction I Prof. Tianhua Zhou Department of Cell Biology Zhejiang University School of Medicine Office hours by appointment tzhou@zju.edu.cn

2 Signal transduction:

3 Key contents for signal transduction: I. Signaling molecules: Diversity, receptors, GTPase switch proteins, adaptor proteins, protein kinases, protein phosphatases II. Signaling Pathways: A. Cell-surface receptor pathways (Receptors that are Ion channels, Signaling through G-protein-coupled receptors, Signaling through Enzyme-linked receptors, Signaling that involved in proteolysis) B. Intracellular receptor pathways (Nitric oxide pathway, Nuclear receptor pathway) III. The regulation of cell signaling: A. The interaction between different signaling pathways (Convergence, Divergence, Crosstalk) B. The adaptation of targeting cells: Receptor sequestration, down-regulation, inactivation, Production of inhibitory protein, Inactivation of signaling protein

4 FUNCTIONS OF CELL COMMUNICATION Cell proliferation Cell differentiation Cell motility Cell survival Cell death

5 CELL COMMUNICATION Gap junctions Cell recognition--communication by plasma membrane-attached proteins Communication by secreted molecules

6 Gap junctions

7 Cell recognition--communication by plasma membrane-bound proteins signaling molecules Target genes (Ligands)

8 Communication by secreted molecules signaling molecules Target genes (Ligands)

9 I. Signaling molecules Ligands: peptides/proteins (growth factors), small lipophilic molecules (steroid hormones), small hydrophilic molecules (epinephrine), gases (nitric oxide) and physical stimuli (lights) etc. Receptors: intracellular receptors and cell surface receptors etc. Intracellular signaling molecules: secondary messengers (camp cgmp IP3 DAG Ca2+), GTPase Switch proteins, protein kinases and phophatases etc. Target genes: cellular metabolism, cell movement and gene expression etc.

10 1. Diversity of signaling

11 2. Receptors Definition: Any protein that specifically binds to another molecules to mediate cell-cell signaling, adhesion, endocytosis or other cellular process. Mostly commonly denotes a protein located in the plasma membrane or cytoplasm that is activated by binding a specific extracellular signaling molecule (ligand), thereby initiating a cellular response. Characteristic: High selectivity, specificity of effector, saturation, reversibility, and high affinity Biochemical feature: binding domain and response domain Types: Intracellular receptors and cell-surface receptors

12

13

14 Experiment: Using cdna expression to identify a receptor

15 Using cdna expression to identify a receptor Purification of mrna Protein expression vectors Promotor Cloning site Amp r Expression vector ori Insert eukaryotic cdna pro cdna insert Amp r ori Insert epitope tag pro cdna insert epitope tag Amp r ori

16 Using cdna expression to identify a receptor

17 3. GTPase Switch proteins GTPases are a large family of enzymes that can bind and hydrolyze GTP. The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. GTPases play an important role in: Signal transduction at the intracellular domain of transmembrane receptors, including recognition of taste, smell and light. Protein biosynthesis at the ribosome. Control and differentiation during cell division. Translocation of proteins through membranes. Transport of vesicles within the cell (GTPases control assembly of vesicle coats).

18 Switching mechanism of GTPase Active GDP GTP exchange GEF, Guanine nucleotide exchange factor GAP, GTPase accelerating protein hydrolysis GTP GDP P i Inactive

19 4. Protein kinases A protein kinase is an enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). This usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. Up to 30% of all proteins may be modified by kinases activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction, the transmission of signals within the cell. The human genome contains about 500 protein kinase genes (kinome); they constitute about 2% of all eukaryotic genes.

20 The chemical activity of a kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three.

21 Because protein kinases have profound effects on a cell, their activity is highly regulated. Kinases are turned on or off by phosphorylation (sometimes by the kinase itself - cis-phosphorylation/autophosphorylation), by binding of activator proteins or inhibitor proteins, or small molecules, or by controlling their location in the cell relative to their substrates. Dysregulation of kinase activity is a frequent cause of disease, particularly cancer, where kinases regulate many aspects that control cell growth, movement and death. Drugs which inhibit specific kinases are being developed to treat several diseases, and some are currently in clinical use, including Gleevec (imatinib) and Iressa (gefitinib).

22 5. Protein phosphatases Protein phosphatases are enzymes that remove phosphate groups that have been attached to amino acid residues of proteins by protein kinases. Whereas a kinase enzymatically adds a phosphate to a protein, a phosphatase's purpose is phosphate removal. It should be noted that phosphate addition and removal do not necessarily correspond to enzyme activation or inhibition, and that several enzymes have separate phosphorylation sites for activating or inhibiting functional regulation. CDK, for example can be either activated or deactivated depending on the specific amino acid residue being phosphorylated. The phosphates are important in signal transduction by regulating the proteins they are attached to. To reverse the regulatory effect, the phosphate has to be removed. This occurs on its own by hydrolysis or is mediated by protein phosphatases.

23 6. Adaptor proteins Src SH3 SH2 Catalytic Y Src family of tyrosine protein kinases Comparison of enzyme sequences revealed 3 domains SH2 binds phosphotyrosine sites SH3 binds proline-rich sequences Identification of adaptor protein (Grb2) Grb2 SH3 SH2 SH3 SH2 domains binding specificity Src-homology 2 (SH2) domains are modules of ~100 amino acids that bind to specific phosphotyrosine (py)- containing peptide motifs. Each SH2 domain has a conserved pocket that recognizes py, and a more variable pocket that binds 3-6 residues C-terminal to the py and confers specificity. Phosphopeptides of optimal sequence bind to SH2 domains with K d s of ~ nm. Binding examples Phosphopeptide SH2 domain protein ligand Src tyrosine kinase ptyr-ala-glu-ile Phospholipase C- ptyr-ile-ile-pro-leu-pro-asp C-terminal SH2 Grb2 adaptor ptyr-val-asn-val

24

25 II. Signaling Pathways Cell-surface receptor pathways Receptors that are Ion channels Signaling through G-protein-coupled receptors Signaling through Enzyme-linked receptors Signaling that involved in proteolysis Intracellular receptor pathways Nitric oxide pathway Nuclear receptor pathway

26 1. Receptors that are Ion channels-- ligand-gated channels Ligands: Neurotransmitters (e.g. acetylcholine, glutamine), physical stimuli (e.g. touch or stretching) etc. Receptors: Four or five subunits with a homologous segment in each subunit lining the ion channel. Signal transduction: A. Localized change in membrane potential due to ion influx or efflux. B. Exchange of cytosolic Ca2+.

27 Chemical synapse

28 Acetylcholine receptor

29 Three conformation of the acetylcholine receptor

30 Ion-channel linked receptors in neurotransmission

31 2. Signaling through G-protein-coupled receptors Ligands: Epinephrine, adenosine, odorant molecules and many others. Receptors: Seven transmembrane a helices; cytosolic domain associated with a membrane-tethered trimeric G protein. Signal transduction: A. Second-messenger pathways involving camp or IP3/DAG. B. Linked ion channels C. MAP kinase pathway

32 Receptor / Trimeric G protein / effector molecule Trimeric G proteins consist of, and subunits subunit binds GTP and has GTPase activity

33 Major classes of mammalian trimeric G proteins and their effectors

34 General structure of G protein-coupled receptors All G protein-coupled receptors have seven transmembranespanning regions This family of proteins includes receptors for many hormones, neurotransmitters and odorant receptors

35 Characterization of the region determining specificity of G protein binding

36 Events leading to effector activation

37 Second messengers

38 camp as a second messenger G S -coupled receptor activates AC G i -coupled receptor inhibits AC G subunits are identical Formation G GTP in both cases is the same G s or G i interact differently with AC camp is a second messenger that activates camp-dependent protein (PKA)

39 Activation of transcription by Gs-coupled receptors 1 - Stimulation of AC 2 - PKA activation 3 - Translocation to nucleus 4 - Transcription factor CREB-P 5 - CREB-P associates with co-activator 6 - Target genes

40 Regulation of glycogen metabolism

41

42 IP3/DAG as a second messenger Involved in transducing information from cell surface receptors Second messengers from phosphatidylinositol PLC IP 3 + DAG DAG remains in membrane IP 3 cytoplasmic

43 Phosphatidylinositol signaling Protein kinase C Required Ca ++ and phosphatidylserine for activity Ca ++ required in micromolar range DAG lowered Ca + requirement to nanomolar range Activation of PKC Release of DAG (membrane-bound) translocated PKC to membrane and resulted in activation IP 3 opens calcium channels Two-step carcinogenesis Initiation - carcinogen Promotion - tumor promoter (phorbol esters) PKC is a major phorbol ester receptor

44 G protein-couple receptors also activate phospholipase C ( ) Second messengers from phosphatidyl inositol

45 The major signaling pathways activated by GPCRs and RTKs

46

47 3. Signaling through Enzyme-linked receptors

48 3.1 Receptor tyrosine kinase pathway Ligands: Insulin, epidermal growth factor (GF), Fibroblast GF, neurotrophins and other GFs. Receptors: Single transmembrane α helix; intrinsic protein tyrosine kinase activity in cytosolic domain; dimerization and phosphorylation induced by binding to ligand. Signal transduction: A. MAP kinase pathway B. IP3/DAG pathway. C. PI-3 kinase pathway

49 Nobel Prize for discovery of growth factors Peptide growth factors Rita Levi-Montalcini 1950: Study of transplantable mouse sarcoma Grafted the tumor on developing chicken embryo Embryo sensory ganglia innervated the transplant Sensory and sympathetic nerve fibers invaded the tumor and branched along the tumor cells but did not establish synaptic junctions Rita Levi-Montalcini (c. 1986) b Under these conditions, the embryo showed aberrant growth and distribution of nerve fibers This suggested the tumor released a humoral factor that acts on sensory and sympathetic ganglia Purified nerve growth factor (NGF) Stanley Cohen 1956: Promotes 1-10 ng Increases ganglia by enhancing differentiation and preventing cell death Stanley Cohen (c. 1986) b.1922 Promotes differentiation of tumor cells such as neuroblastoma cells in vitro Removes NGF degeneration

50 Epidermal Growth Factor Stanley Cohen Used mouse submaxillary gland as source of NGF Noted another activity Factor caused precocious incisor eruption, early eyelid opening and lung maturation - epithelial cells Purification with these assays

51 The structure of Receptor tyrosine kinase

52 Diversity of receptor structure

53 Different receptors interact with downstream molecules with unique SH2 domains

54 Activation of PLC after activation of EGF receptor PLC is activated by EGF. EGF activates MAP kinase. EGF activates PI3 kinase.

55 MAP kinase pathway Activation of Ras after activation of EGF receptor Grb2 is an adaptor protein Sos is a guanine nucleotide exchange factor Sos displaces GDP

56 Activation of the MAP kinase pathway Raf Mek MAP kinase

57 Induction of gene transcription by activated MAP kinase

58 IP3/DAG pathway is activated by EGF

59 Phosphatidylinositol 3 kinase (PI3K) pathway Identified by its association with activated PDGFR Consists of 85kDa and 110kDa subunits Phosphorylated inositol at the 3 position of the inositol ring Activation of phosphatidylinositol kinase 1 (PDK1)

60 Generation of PI3 phosphates Generation of IP3/DAG

61 Phosphatidylinositol pathway

62 Recruitment and activation of PKB by phosphatidyl inositols In unstimulated cell PKB is in cytosol Formation of PI 3, 4-biphosphate The PH domain of PKB docks to the 3-phosphate partial activation PDK1 also binds P I3, 4-bisphosphate PDK1 phosphorylation results in activation of PKB PDK is phosphoinositol dependent kinase PKB, Akt I, influences cell survival

63 PI3 Kinase signaling

64

65 The interactome map within cells

66

67

68 Experiment: Co-immunopreciptation to detect downstream players A = unstimulated cell Antibody v. receptor + Extract of cells B = stimulated cell + Extract of cells Antibody v. receptor Receptor Subjected tor Western analysis Wash to remove noninteracting proteins Antibodies v. protein X and receptor Receptor Subjected to Western analysis? Wash to remove noninteracting proteins Antibodies v. protein X and receptor Protein X? Co-immunoprecipitated protein Co-immunoprecipitated protein

69 Breakout Based on the data above, we suggest that band X is A). A protein associated with receptor. B). Antibody. C). Both A and B. D). None of them.

70 The major signaling pathways activated by GPCRs and RTKs

71 Welcome to Bio-Lab!

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