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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 December 3, 2024, from https://doi.org/10.69645/RCIW3639.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Linda M. Hendershot has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
A selection of talks on Cell Biology
Transcript
Please wait while the transcript is being prepared...
0:00
Hi, I'm Linda Hendershot,
The Department of Tumor Cell Biology at
St. Jude Children's Research Hospital in Memphis, Tennessee.
I'll be talking about the chaperon systems of the endoplasmic reticulum.
0:14
The ability of cells to communicate with each other and their environment in
specific ways is essential to survival in multicellular organisms.
0:24
One of the primary ways this is done is through proteins
expressed on the cell surface or secreted from the cell.
For example, a damaged cell or tumor cell,
which requires additional nutrients or oxygen,
has the ability to secrete pro-angiogenic factors which will bind to
endothelial cells and stimulate the production of
blood vessel and oxygen flow to the tumor cell.
0:53
Another example is direct cell to cell communication.
For example, a virus-infected cell is recognized by
a T-cell of the immune system by an antigen is expressed on the cell surface,
which can induce the T-cells to kill the virus-infected cell.
1:12
Another example is the secretion of effector molecules like antibodies from plasma cells,
which can target bacteria for destruction.
1:24
Another example is the use of proteins for cellular communication can be seen
in the migration of cells throughout the body or homing into specific tissues.
For example, a B cell,
which can be synthesized in the fetal liver or in the bone marrow,
was turned to a lymph node,
which occurs at the expression of proteins on
the B cell surface that interacts with proteins on the surface of the lymph node.
The cell surface and secreted proteins are