Select the best explanation of the unfolded protein response (UPR):O A. The UPR senses misfolded proteins through detection of proteins tagged with polyubiquitin chains and sends them for degradation in the lysosomeB. The UPR senses misfolded proteins through recognition of specific oligosaccharide conformations and sends them for degradation via theproteasomeC. The UPR senses high levels of misfolded proteins in the ER and activates ubiquitin ligases to add ubiquitin to the misfolded proteins and target themfor secretion from the cell.D. The UPR senses ER stress in the form of high levels of misfolded proteins and signals the cell to halt translation and induces expression of ERchaperones

When the protein is completely formed it is folded accordingly yo form a biologically active protein…

Select the best explanation of the unfolded protein response (UPR): O A. The UPR senses misfolded proteins through detection of proteins tagged with polyubiquitin chains and sends them for degradation in the lysosome O B. The UPR senses misfolded proteins through recognition of specific oligosaccharide conformations and sends them for degradation via the proteasome OC. The UPR senses high levels of misfolded proteins in the ER and activates ubiquitin ligases to add ubiquitin to the misfolded proteins and target them for secretion from the cell. O D. The UPR senses ER stress in the form of high levels of misfolded proteins and signals the cell to halt translation and induces expression of ER chaperones

Select the best explanation of the unfolded protein response (UPR): O A. The UPR senses misfolded proteins through detection of proteins tagged with polyubiquitin chains and sends them for degradation in the lysosome O B. The UPR senses misfolded proteins through recognition of specific oligosaccharide conformations and sends them for degradation via the proteasome OC. The UPR senses high levels of misfolded proteins in the ER and activates ubiquitin ligases to add ubiquitin to the misfolded proteins and target them for secretion from the cell. O D. The UPR senses ER stress in the form of high levels of misfolded proteins and signals the cell to halt translation and induces expression of ER chaperones

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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The affinity of integrins for matrix components canbe modulated by changes to their cytoplasmic domains:a process known as inside-out signaling. You have iden-tified a key region in the cytoplasmic domains of αIIbβ3integrin that seems to be required for inside-out signaling(Figure Q19–3). Substitution of alanine for either D723in the β chain or R995 in the α chain leads to a high levelof spontaneous activation, under conditions where thewild-type chains are inactive. Your advisor suggests thatyou convert the aspartate in the β chain to an arginine(D723R) and the arginine in the α chain to an aspartate(R995D). You compare all three α chains (R995, R995A,and R995D) against all three β chains (D723, D723A, andD723R). You find that all pairs have a high level of sponta-neous activation, except D723 vs R995 (the wild type) andD723R vs R995D, which have low levels. Based on theseresults, how do you think the αIIbβ3 integrin is held in itsinactive state?
Indicate (x) if the following statements about synthesis of proteins containing an ER signal sequence are True or False: True False i. Translation is initiated by ribosomes located on the ER membrane The signal recognition particle (SRP) binds a sequence of nonpolar (hydrophobic) amino acids. ii. iii. The ER signal sequence may be cleaved by signal peptidase on the cytoplasmic side of the ER membrane. iv. The part of a transmembrane protein that will ultimately be located outside of the cell is inserted into the lumen of the ER during translation. A stop transfer sequence is a series of polar amino acids that halts translocation of a newly synthesized peptide into the ER lumen.
Predict the location(s) (intracellular or extracelular) and a brief description of WHY based on your knowledge of the transport processes in the following constructs. Assume a start codon is present and include any proteolytic processing that would be likely. 1. A PTS1 C-term peroxisomal targeting seq added to C term of a normally secreted protein with usual N -terminal signal sequence 2. Adding of N-terminal mitochondrial targeting sequence to protein with internal nuclear localization seq. 3. Adding N-terminal signal sequence of secreted protein to N-terminus a mitochondria matrix protein precursor with mitochondrial targeting sequence still present
A current focus of molecular medicine is to trigger or promote apoptosis of specific cells. several components of the apoptotic pathways are being targeted using this approach. for following, state specifically how the treatment would be expected to stimulate or inhibit apoptosis. c. Treatment of cells with organic compounds that enter the cell and bind with high affinity to the active site of Caspase-3
TGF-B Receptor I (RI) phosphorylation of Smad2/3 does all of the following EXCEPT: activate Smad2/3 binding to the Co-Smad Smad4 dissociate intramolecular binding of Smad2/3 MH1 and MH2 domains. RI phosphorylation of Smad2/3 does all of these things. release Smad2/3 from the nucleus into the cytoplasm unmask the Smad2/3 nuclear localization signal (NLS).
For each of the following, describe the path the protein takes to its final destination in the cell.Drawings are strongly recommended!Proteins: 1) Hedgehog (released from the signaling cell), 2) Smoothened, 3) Ci/GliYour answers should include the following if they apply for each protein:o Sorting sequences and how the protein knows where to go at each step (what recognizesdifferent sorting sequences/tags)o How/when the protein is inserted into the membrane (if it is a membrane protein)o What organelles the protein passes through on its way to its final destinationo How the protein is transported (vesicles? translocons? etc.), including a role for microtubuleso How the protein might be modified in each organelle it passes througho What other proteins are involved in transport and how the system is reset to allow for otherproteins to be transported
Explain the mechanism by which the fungal toxin brefeldin A affects retrieval of KDEL-tagged proteins from the cis-Golgi network back to the endoplasmic reticulum.
Describe the role of pH in regulating the interaction between mannose 6-phosphate and the M6P receptor. Why does a rise in endosomal pH lead to the secretion of newly synthesized lysosomal enzymes into the extracellular medium?
Members of the integrin family are the major cell surface receptors for many ECM proteins such as fibronectin. In experimental studies, single integrin heterodimers have been found to assume more than one structural conformation. Describe the relationship between integrin structures and their activities.
Measure the uptake of leucine by epithetial cells of the mouse intestine. Measurements of the rate of update of L-leucine, D-Leucine, and L-valine , with and without Na+ in the assay were perform and yield different results (see table below). A) What can you conclude about the properties and mechanism of leucine transporter? B) Would you expect L-leucine uptake to be inhibited by Ouabain, which is a cardiac glycoside drug treatment?
For each of the following, describe the path the protein takes to its final destination in the cell.Drawings are strongly recommended! If you need more space, you can use a separate sheet ofpaper. Proteins: 1) Hedgehog (released from the signaling cell), 2) Smoothened, 3) Ci/GliYour answers should include the following if they apply for each protein:o Sorting sequences and how the protein knows where to go at each step (what recognizesdifferent sorting sequences/tags). How/when the protein is inserted into the membrane (if it is a membrane protein) What organelles the protein passes through on its way to its final destination. How the protein is transported (vesicles? translocons? etc.), including a role for microtubules.How the protein might be modified in each organelle it passes through. What other proteins are involved in transport and how the system is reset to allow for otherproteins to be transported.
Which statement about the M6P receptor is true/accurate? Answers: It is involved in retrieval of ER resident proteins from the Golgi and transport back to the ER. Due to no difference in pH in the lumen of each, it has the same affinity for M6P in the Golgi as in the endosome. Due to a slight difference in pH in the lumen of each, it has a high affinity for M6P in the Golgi and a low affinity for M6P in the endosome. Due to a slight difference in pH in the lumen of each, it has a low affinity for M6P in the Golgi and a high affinity for M6P in the endosome.