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1. Introduction
2. Communication between cells is essential
3. Angiogenesis
4. Direct cell to cell communication
5. Secretion of effector molecules
6. Cell migration/homing
7. Proteins are synthesized in the ER
8. Folding can begin before translation is complete
9. Folding is guided by individual amino acids
10. Role of molecular chaperones in the ER (1)
11. Role of molecular chaperones in the ER (2)
12. Molecular chaperone families of mammalian ER
13. BiP was the first ER chaperone to be identified
14. Antibody formation
15. BiP is a soluble Hsp70 protein of the ER
16. ATPase and DnaK peptide binding domains
17. Peptide sequences that bind to BiP
18. Light chains cover a hydrophobic patch on CH1
19. The formation of disulfide bonds
20. CH1 domain remains unfolded
21. CH1 domain is intrinsically disordered
22. ATPase cycle of BiP
23. ATPase activity of BiP is required for folding
24. Disruption of BiP/GRP78 gene in mice
25. Highly virulent subtilase toxin
26. BiP functions in ER
27. BiP recruitment to substrates by ERdj proteins
28. BiP forms a complex with other ER chaperones (1)
29. DnaJ family members subdivide into 3 groups
30. Mammalian ER DnaJ proteins
31. Role of ERdjs in the ER
32. Mutations in Sec63(ERdj2)
33. BiP must release for substrates to fold (1)
34. Gal-4-BiP ATPase domain fusion protein
35. BAP/Sil1 serves as a nucleotide releasing factor
36. BiP must release for substrates to fold (2)
37. Potential consequences of BAP/Sil1 loss
38. Marinesco-Sjogren syndrome
39. Sil1 mutations affect BiP interactions
40. Sil1: 3 mutations affect the C-terminal amino acids
41. Effects of the loss of Sil1 C-terminal amino acids
42. Why isn't Sil1 loss lethal if BiP loss is?
43. The family of large Hsp70 proteins
44. Lhs1 has nucleotide exchange activity for BiP
45. The Sil1 KO mouse
46. UPR is activated in Sil1 null mouse cerebellum
47. GRP170 appears to have two functions (1)
48. Sil1 is highly expressed in secretory tissues
49. BiP forms a complex with other ER chaperones (2)
50. GRP94 is one of the resident ER proteins
51. GRP94 is required for Toll-like receptor transport
52. GRP94 is an essential gene
53. ES cells derived from GRP94 null cells
54. IGF-II is an essential client of GRP94
55. GRP94 is required for glycoprotein degradation
56. The ER has two resident immunophilins
57. Cyclophilin B accelerates proline isomerization
58. Which is necessary for Ig assembly & secretion
59. BiP forms a complex with other ER chaperones (3)
60. pERp1 is a lymphoid specific chaperone
61. Sequential action of molecular chaperones

Topics Covered

• Communication between cells
• Angiogenesis
• Secretion of effector molecules
• Cell migration/homing
• Proteins synthesis & folding
• Molecular chaperone families in the ER
• Antibody formation
• BiP: a soluble Hsp70 protein
• ATPase and DnaK peptide binding domains
• CH1 domain
• The formation of disulfide bonds
• ATPase cycle of BiP
• Disruption of BiP/GRP78 gene in mice
• Highly virulent subtilase toxin
• BiP functions in ER
• ER DnaJ proteins
• Gal-4-BiP ATPase domain fusion protein
• BAP/Sil1: a nucleotide releasing factor
• Potential consequences of BAP/Sil1 loss and mutations
• The family of large Hsp70 proteins
• The two functions of GRP170
• GRP94 as an essential gene- Immunophilins
• lymphoid specific chaperone: pERp1

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Hendershot, L.M. (2012, February 20). Chaperone systems of the endoplasmic reticulum [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved October 15, 2019, from https://hstalks.com/bs/2225/.

Publication History

• Published on February 20, 2012

Financial Disclosures

• Prof. Linda M. Hendershot has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.