1. Copyright (c) by W. H. Freeman and Company 17.3 The rough ER is an extensive interconnected series of flattened sacs Figure 17-11

2. Copyright (c) by W. H. Freeman and Company 17.3 Secretory proteins are found in the ER lumen immediately after synthesis Figure 17-12

3. Copyright (c) by W. H. Freeman and Company 17.3 Overview of the secretory pathway Figure 17-13 cisternal progression

4. Copyright (c) by W. H. Freeman and Company 17.3 Many experiments on the secretory pathway have relied on cells specialized for the secretion of certain proteins

5. Copyright (c) by W. H. Freeman and Company Box 4.5

6. Copyright (c) by W. H. Freeman and Company 17.3 Analysis of yeast mutants defined the major steps in the secretory pathway Figure 17-14

7. Copyright (c) by W. H. Freeman and Company Fig. 4.13

8. Copyright (c) by W. H. Freeman and Company Fig. 4.14

9. Copyright (c) by W. H. Freeman and Company 17.4 A signal sequence on nascent secretory proteins targets them to the ER and then is cleaved off

10. Copyright (c) by W. H. Freeman and Company 17.4 The cotranslational import of proteins into the ER is studied with microsomes Figure 17-15

11. Copyright (c) by W. H. Freeman and Company 17.3 Some acronyms  SRP - signal recognition particle Particle made of 1 RNA and six proteins which binds the signal sequence on newly made proteins  SRP receptor - ER protein which binds SRP  TRAM - translocating chain-associated membrane (also translocon) takes the protein across the ER membrane

12. Copyright (c) by W. H. Freeman and Company 17.4 Two proteins initiate the interaction of signal sequences with the ER membrane Figure 17-16

13. Copyright (c) by W. H. Freeman and Company 17.4 Structure of the signal recognition particle (SRP) Figure 17-17

14. Copyright (c) by W. H. Freeman and Company 17.4 Polypeptides move through the translocon into the ER lumen Figure 17-18

15. Copyright (c) by W. H. Freeman and Company Fig. 4.15

16. Copyright (c) by W. H. Freeman and Company 17.4 GTP hydrolysis powers protein transport into the ER in mammalian cells Figure 17-20

17. Copyright (c) by W. H. Freeman and Company 17.5 Topologies of some integral membrane proteins synthesized on the rough ER Figure 17-21

18. Copyright (c) by W. H. Freeman and Company Fig. 4.17

19. Copyright (c) by W. H. Freeman and Company 17.5 Most nominal cytosolic transmembrane proteins have an N-terminal signal sequence and an internal topogenic sequence Figure 17-22

20. Copyright (c) by W. H. Freeman and Company 17.5 A single internal topogenic sequence directs insertion of some single-pass transmembrane proteins Figure 17-23

21. Copyright (c) by W. H. Freeman and Company 17.5 Multipass transmembrane proteins have multiple topogenic sequences Figure 17-24

22. Copyright (c) by W. H. Freeman and Company 17.5 After insertion into the ER membrane, some proteins are transferred to a GPI anchor Figure 17-25

23. Copyright (c) by W. H. Freeman and Company 17.5 After insertion into the ER membrane, some proteins are transferred to a GPI anchor Figure 17-25

24. Copyright (c) by W. H. Freeman and Company 17.6 Post-translational modifications and quality control in the rough ER  Newly synthesized polypeptides in the membrane and lumen of the ER undergo five principal modifications  Formation of disulfide bonds  Proper folding  Addition and processing of carbohydrates  Specific proteolytic cleavages  Assembly into multimeric proteins

25. Copyright (c) by W. H. Freeman and Company 17.6 Disulfide bonds are formed and rearranged in the ER lumen Figure 17-26

26. Copyright (c) by W. H. Freeman and Company Fig. 4.18

27. Copyright (c) by W. H. Freeman and Company 17.6 Correct folding of newly made proteins is facilitated by several ER proteins Figure 17-27

28. Copyright (c) by W. H. Freeman and Company 17.6 ER-resident proteins often are retrieved from the cis-Golgi Figure 17-29

29. Copyright (c) by W. H. Freeman and Company 17.7 Different structures characterize N- and O-linked oligosaccharides Figure 17-30

30. Copyright (c) by W. H. Freeman and Company 17.7 The immediate precursors in the synthesis of oligosaccharides are nucleoside diphosphate or monophosphate sugars Figure 17-31

31. Copyright (c) by W. H. Freeman and Company 17.7 Specific sugars are linked by specific glycosyltransferases Figure 17-32

32. Copyright (c) by W. H. Freeman and Company 17.7 Sugar nucleotides and free nucleotides are exchanged by antiporters in the ER membrane Figure 17-33

33. Copyright (c) by W. H. Freeman and Company 17.7 ABO blood type is determined by two glycosyltransferases Figure 17-34

34. Copyright (c) by W. H. Freeman and Company 17.7 ABO blood groups

35. Copyright (c) by W. H. Freeman and Company 17.7 A common preformed N-linked oligosaccharide is added to many proteins in the rough ER Figure 17-35

36. Copyright (c) by W. H. Freeman and Company 17.7 Addition and initial processing of N- linked oligosaccharides in the rough ER Figure 17-36

37. Copyright (c) by W. H. Freeman and Company Fig. 4.27

38. Copyright (c) by W. H. Freeman and Company Fig. 4.20

39. Copyright (c) by W. H. Freeman and Company Fig. 4.28

40. Copyright (c) by W. H. Freeman and Company Fig. 4.22

41. Copyright (c) by W. H. Freeman and Company Box 4.4

42. Copyright (c) by W. H. Freeman and Company Fig. 4.23 Developing wheat endosperm

43. Copyright (c) by W. H. Freeman and Company Fig. 4.24

44. Copyright (c) by W. H. Freeman and Company Fig. 4.25

45. Copyright (c) by W. H. Freeman and Company Fig. 4.29 extensin

46. Copyright (c) by W. H. Freeman and Company 17.7 Modifications to N-linked oligosaccharides are completed in the Golgi complex Figure 17-38 Oligosaccharides may promote folding and stability of glycoproteins

47. Copyright (c) by W. H. Freeman and Company Golgi and post-Golgi protein sorting  Sequences in the membrane-spanning domain cause the retention of proteins in the Golgi  Different vesicles are used for continuous and regulated protein secretion

48. Copyright (c) by W. H. Freeman and Company Fig. 4.21

49. Copyright (c) by W. H. Freeman and Company 17.10 Components that participate in budding of coated vesicles Figure 17-51

50. Copyright (c) by W. H. Freeman and Company Figure 17-60

51. Copyright (c) by W. H. Freeman and Company 17.10 A clathrin-coated pit on the cytosolic face of the plasma membrane Figure 17-35

52. Copyright (c) by W. H. Freeman and Company 17.10 Structure of a clathrin-coated vesicle Figure 17-53

53. Copyright (c) by W. H. Freeman and Company 17.10 Model for formation of a clathrin-coated pit and selective incorporation of integral membrane proteins Figure 17-54

54. Copyright (c) by W. H. Freeman and Company 17.10 GTP hydrolysis by dynamin is required for pinching off of clathrin-coated vesicles Figure 17-55

55. Copyright (c) by W. H. Freeman and Company 17.10 COP I vesicles mediate retrograde transport within the Golgi and from the Golgi back to the ER Figure 17-56

56. Copyright (c) by W. H. Freeman and Company 17.10 Model for formation of COP I-coated vesicles Figure 17-58

57. Copyright (c) by W. H. Freeman and Company 17.10 Specific fusion of intracellular vesicles involves a conserved set of fusion proteins Figure 17-59

58. Copyright (c) by W. H. Freeman and Company Box 4.6B