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These flashcards cover key terminology and concepts from the lecture on ER, peroxisomes, and mitochondrial transport.
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GPI-anchored proteins
Proteins attached to the cell surface via a glycosylphosphatidylinositol anchor, often involved in signaling.
N-glycosylation
A post-translational modification where oligosaccharides are added to asparagine residues of proteins in the ER.
Unfolded Protein Response (UPR)
A cellular response triggered by excessive misfolded proteins in the ER, aiming to restore normal function.
Chaperones
Proteins that assist in the proper folding of other proteins and prevent aggregation.
Disulfide isomerase
An enzyme that rearranges disulfide bonds in misfolded proteins to assist in their correct folding.
Proteasomal degradation
A process in which misfolded or unneeded proteins are tagged and broken down by the proteasome.
Bortezomib
A proteasome inhibitor that is used clinically to treat multiple myeloma by inducing apoptosis in malignant cells.
Scramblase
A protein that facilitates the ATP-independent movement of lipids across the lipid bilayer, contributing to lipid asymmetry.
Flippases
ATP-dependent enzymes that transport specific phospholipids to one side of the membrane, contributing to lipid asymmetry.
β-oxidation
A metabolic process by which fatty acids are broken down in peroxisomes to generate energy.
TOM & TIM complexes
Protein complexes that assist in transporting nuclear-encoded proteins across the mitochondrial membranes.
Signal peptide
A short peptide sequence that directs the transport of proteins to specific locations within the cell.
Calnexin
A chaperone protein in the ER that binds to glycoproteins to facilitate proper folding.
E3 ubiquitin ligase
An enzyme that tags misfolded proteins with ubiquitin, marking them for degradation by the proteasome.
Glucosyl transferase
An enzyme that adds glucose residues to glycan chains attached to partially folded proteins to aid in quality control.