UCI SOM Liu
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| Cytosolic ribosomal polypeptides can end up where | cytosol, mitochondrion, peroxisome, and nucleus
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| Rough ER polypeptides can go where | ER, golgi, secretory vesicles, plasma membrane, endosome, and lysosome
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| Which membranes use membrane translocation for protein transport | mitochondrion, peroxisome and ER
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| How do proteins get inside the nucleus | gated transport
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| How do proteins transport into the golgi, secretory vesicles, plasma membrane, endosomes, and lysosomes | vesicular transport
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| Where are proteins glycosylated | ER and golgi
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| In which cell locations are proteins not glycosylated | cytosol, mitochondrion, peroxisome, and nucleus
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| Proteins destined to mitochondria have what | amino terminal leader sequence (lots of positive charged AA’s
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| Is translocation into the mitochondria co-translational | no
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| What’s different about mitochondrial protein translocation | protein is unfolded
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| Pre- sequence | signal peptide on nearly all secreted peptides
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| 6 signal sequence features | 1)on N-terminus 2)12-35 AA long 3)Met is first AA 4)central group of hydrophobic AA 5)at least one + charged AA near N-terminus 6)cleaved off at Ala by signal peptidase
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| what halts translation in ER bound proteins | SRP
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| SRP features | 6 polypeptides, 7S RNA; the 54k subunit contains 12% methionine to bind the hydrophobic signal peptides
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| When is the SRP-imposed block released | after docking to the ER on the SRP receptor
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| When is the signal peptide cleaved off in the ER | once ER translocation is complete
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| When is the protein glycosylated in the ER | immediately
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| What kind of signal does an integral membrane protein have | an internal halt- or stop- transfer signal.
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| Where is the glycosylated part of a protein NEVER located | in the cytoplasm
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| Glycoproteins are suggested to contribute to what | metastasis of cancers
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| 3 classes of glycoproteins | O-linked, N-linked, GPI-anchored
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| o-linked linkage | GalNAc-Ser/Thr
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| n-linked linkage | GlcNAc-Asn
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| GPI-anchored linkage | oligosaccharide which is linked to the protein at the C-terminus with phosphorylethanolamine and is also linked to a phosphatidylinositol (PI)
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| 3 classes of o-glycosidic linkages | 1)GalNAc-Ser/Thr; most common (mucin) 2)proteoglycans contain Gal-Gal-Xyl-Ser/Thr then long repeating disaccharides (synovial fluid) 3)Collagen contains Gal-hydroxylysine
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| where does addition of sugar residues occur in o-glycosylation and when does it occur | occurs in the ER and is cotranslational.
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| Three classes of N-linked glycoproteins | complex, hybrid, and high-mannose
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| Common N-linked structures | Asn-2GlcNAc-3Man
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| When and where are N-linked glycoproteins glycosylated | in the ER wherever Asn-X-Thr/Ser occurs (X is any AA except Pro)
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| Where does the oligosaccharide for N-linked glycoproteins come from | Dolichol-P-P-oligosaccharide
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| when does Dolichol-P-P-oligosaccharide transfer on | co-translationally
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| Tunicamycin | inhibits an enzyme in the synthesis of dolichol-oligosaccharide donor
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| How is the oligosaccharide for N-linked glycoproteins changed | step-wise rxns
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| Where do changes to the oligosaccharide for N-linked glycoproteins occur | ER and Golgi
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| GPI anchor synthesis | assembled independently then transferred near the C-terminus of protein accompanied by C-terminus end cleavage
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| What determines blood type | carb structures on cell surface
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| Blood type O | nothing added to Gal
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| Blood type A | GalNAc added to Gal
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| Blood type B | Gal added to Gal
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| 3 types of coated vesicles | clathrin-coated, COPI-coated, and COPII-coated
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| major coat proteins | clathrin
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| what does clathrin do | provides physical budding force and vesicle formation
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| triskelion | clathrin 3 heavy chain and 3 light chain form a triskelion
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| adaptin | coat protein that’s a molecular link between clathrin and transmembrane receptors
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| what pinches off the clathrin coated bud using GTP | dynamin
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| COPI and COPII require | GTPase
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| Sar1-GDP | used in COPII; GDP-GTP to become active and lodges itself into the ER membrane
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| ARF-GDP | used in COPI; responsible for COPI and clathrin coat assembly at golgi membranes
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| COPI | golgi to ER
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| COPII | ER to Golgi
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| T-SNARE | target protein on membrane that v-snare finds
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| v-SNARE | on vesicle and finds t-snare
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| Rab protein | GTPase family protein that monitors SNARE fitting and hydrolyzes the GTP to lock the SNAREs together
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| Vesicular tubular cluster | the group of vesicles going from the ER to Golgi
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| How do vesicular tubular clusters move | along microtubules
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| ER retrieval signal | signal sequence that binds to COPI and are packaged for retrograde transport to the ER
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| KDEL | lys-asp-glu-leu; ER retrieval sequence; bind to KDEL receptors to be returned to ER
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| Where do regulated and constitutive secretory pathways diverge | TGN
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| What supplies the plasma membrane with proteins and lipids | constitutive secretory pathway
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| Regulated secretory pathway steps | selected proteins are sorted, packaged in clathrin coated vesicles at TGN, proteolytic cleavage occurs, triggered release in response to cell signal
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| Rab3 | a synaptic vesicle specific G-protein
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| What cells do phagocytosis | macrophages and neutrophils
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| Formyl-methionyl-peptides | macrophages recognize and phagocytize anything starting with this b/c prokaryotic proteins start with formyl-methionyl
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| Opsonozation | a bacterium must be opsonized (covered in IgG’s that are recognized by Fc receptor on macrophage or neutrophil) before it can be engulfed
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| Pinocytocis occurs in which cells | all
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| Nonselective pinocytosis | fluid-phase
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| Receptor-mediated pinocytosis | uptake of macromolecules; occurs in coated pits
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| 3 outcomes of receptor mediated endocytosis | recycles, degraded, transcytosis
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| 2 fxns of lysosomes | degradation of endocytic material and autophagy
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| residual body | lysosome when the enzymes are used up
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| with what are lysosomal enzymes tagged in the CGN | mannos-6-phosphate
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| M6P receptor proteins | transport lysosomal hydrolase from TGN to late endosome
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| I-cell disease | Inclusion cell disease;lack N-acetylglucosaminephosphotranspherase deficiency (lysosomal hydrolases get sent out of cell); lysosomes accumulate partly digested material (lots of inclusion bodies)
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