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- The Endoplasmic Reticulum: A Regulator of Calcium Homeostasis and Lipid Metabolism
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1. The endoplasmic reticulum: protein folding and control of calcium homeostasis
- Prof. Marek Michalak
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2. Regulation and role of mitochondrial Ca2+ homeostasis
- Prof. Rosario Rizzuto
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3. The InsP3 receptor calcium release channel
- Prof. J. Kevin Foskett
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4. Lipid metabolism and the endoplasmic reticulum
- Prof. Luis Agellon
- The Endoplasmic Reticulum: A Protein Synthesis Factory
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5. Endoplasmic reticulum, protein synthesis and translocation machinery
- Dr. Christopher Nicchitta
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6. Glycoprotein maturation and quality control in the endoplasmic reticulum
- Prof. Daniel Hebert
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7. Membrane transport from the endoplasmic reticulum
- Dr. Benjamin Glick
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8. The endoplasmic reticulum in plants
- Dr. Jurgen Denecke
- The Endoplasmic Reticulum and the Secretory Pathway
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9. The endoplasmic reticulum: the unfolded protein response
- Prof. Randal Kaufman
- Archived Lectures *These may not cover the latest advances in the field
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10. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurones
- Prof. Alexei Verkhratsky
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11. The endoplasmic reticulum as a calcium gateway in programmed cell death
- Prof. Nicolas Demaurex
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12. The endoplasmic reticulum as a most efficient antibody factory
- Prof. Roberto Sitia
Printable Handouts
Navigable Slide Index
- Introduction
- Intracellular protein trafficking
- Protein maturation in the secretory pathway
- How proteins first encounter the secretory pathway
- Processes in the ER
- Protein modifications (1)
- Protein modifications (2)
- Alteration of residues
- ER glycoforms
- The glyco-code of the ER
- Calnexin and calreticulin (1)
- Crystal structure of calnexin
- Calnexin and calreticulin binding to HA
- Calnexin binding cycle (1)
- Calnexin/calreticulin functions
- Co-translational folding
- Average protein synthesis time
- Influenza hemagglutinin
- Oxidation of HA
- HA truncations
- A model for HA maturation
- Type I membrane proteins
- Proteins protecting the nascent chain
- Qaulity control
- Loss of function vs. gain of toxicity
- Diseses involving ER folding and quality control
- Tyrosinase is a bona fide ERAD substrate
- Tyr(C85S) is retained in the ER
- Functional vs. structural
- Structural determinants that cause retention
- ER retention signals
- Calnexin binding cycle (2)
- GT, or UDP-glucose glycoprotein
- Degradation of misfolded proteins
- Importance of carbohydrate trimming
- EDEM1, a putative mannose-binding protein
- EDEM1 and degradation of ERAD substrates
- EDEM1 extracts proteins from the calnexin cycle
- Summary-maturation and qaulity control in the ER
Topics Covered
- Protein maturation in the secretory pathway
- ER glycoforms
- The glyco-code of the ER
- Calnexin and calreticulin
- Cotranslational folding
- Influenza hemagglutinin
- Oxidation of HA
- HA truncations
- Type I membrane proteins
- Disease states involving ER folding and quality control
- Structural determinants that cause retention
- ER retention signals
- Calnexin binding cycle
- GT or UDP glucose glycoprotein: glycosyltransferase
- Degradation of misfolded proteins
- Carbohydrate trimming
- EDEM1 functions
Talk Citation
Hebert, D. (2007, October 1). Glycoprotein maturation and quality control in the endoplasmic reticulum [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved May 9, 2025, from https://doi.org/10.69645/KAXE9724.Export Citation (RIS)
Publication History
- Published on October 1, 2007
Financial Disclosures
- Prof. Daniel Hebert has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
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