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Printable Handouts
Navigable Slide Index
- Introduction
- Communication between cells is essential
- Angiogenesis
- Direct cell to cell communication
- Secretion of effector molecules
- Cell migration/homing
- Proteins are synthesized in the ER
- Folding can begin before translation is complete
- Folding is guided by individual amino acids
- Role of molecular chaperones in the ER (1)
- Role of molecular chaperones in the ER (2)
- Molecular chaperone families of mammalian ER
- BiP was the first ER chaperone to be identified
- Antibody formation
- BiP is a soluble Hsp70 protein of the ER
- ATPase and DnaK peptide binding domains
- Peptide sequences that bind to BiP
- Light chains cover a hydrophobic patch on CH1
- The formation of disulfide bonds
- CH1 domain remains unfolded
- CH1 domain is intrinsically disordered
- ATPase cycle of BiP
- ATPase activity of BiP is required for folding
- Disruption of BiP/GRP78 gene in mice
- Highly virulent subtilase toxin
- BiP functions in ER
- BiP recruitment to substrates by ERdj proteins
- BiP forms a complex with other ER chaperones (1)
- DnaJ family members subdivide into 3 groups
- Mammalian ER DnaJ proteins
- Role of ERdjs in the ER
- Mutations in Sec63(ERdj2)
- BiP must release for substrates to fold (1)
- Gal-4-BiP ATPase domain fusion protein
- BAP/Sil1 serves as a nucleotide releasing factor
- BiP must release for substrates to fold (2)
- Potential consequences of BAP/Sil1 loss
- Marinesco-Sjogren syndrome
- Sil1 mutations affect BiP interactions
- Sil1: 3 mutations affect the C-terminal amino acids
- Effects of the loss of Sil1 C-terminal amino acids
- Why isn't Sil1 loss lethal if BiP loss is?
- The family of large Hsp70 proteins
- Lhs1 has nucleotide exchange activity for BiP
- The Sil1 KO mouse
- UPR is activated in Sil1 null mouse cerebellum
- GRP170 appears to have two functions (1)
- Sil1 is highly expressed in secretory tissues
- BiP forms a complex with other ER chaperones (2)
- GRP94 is one of the resident ER proteins
- GRP94 is required for Toll-like receptor transport
- GRP94 is an essential gene
- ES cells derived from GRP94 null cells
- IGF-II is an essential client of GRP94
- GRP94 is required for glycoprotein degradation
- The ER has two resident immunophilins
- Cyclophilin B accelerates proline isomerization
- Which is necessary for Ig assembly & secretion
- BiP forms a complex with other ER chaperones (3)
- pERp1 is a lymphoid specific chaperone
- 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
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 January 17, 2021, from https://hstalks.com/bs/2225/.Publication History
Financial Disclosures
- Prof. Linda M. Hendershot has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Chaperone systems of the endoplasmic reticulum
Published on February 20, 2012
49 min