The mannose 6-phosphate (M6P) receptorsare crucial for delivering lysosomal proteinsto lysosomes, while the KDEL receptors areimportant to send the ER resident proteinsback to the ER. Which of the followingstatements is INCORRECT regarding theM6P receptors and the KDEL receptors?They both shuttle back and forth betweendifferent membrane-enclosedcompartments.They are both transmembrane proteins.They both release their soluble bindingtargets at a lower pH.They both prevent the escape of proteins tothe cell exterior by the "default" pathway

Vesicular transport is responsible for molecular traffic between specific membrane-enclosed…

Answered: The mannose 6-phosphate (M6P) receptors…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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If cells are treated with colchicine, a drug that promotes microtubule disassembly, the location of the ER and Golgi both change dramatically. Rather than being spread out quite widely through the cytoplasm, the ER appears to collapse into the area near the nucleus. (Recall that the ER membrane and the outer nuclear envelope are continuous with one another). In contrast, the Golgi stacks disperse from their usually more compact, central location to areas all over the cell. However, if colchicine is removed, and microtubules are allowed to reassemble, both organelles eventually return to their normal distribution in the cells. How do you account for the change in distribution of the ER & Golgi when microtubules are depolymerized? What protein(s), other than tubulins, allow normal cellular organization to be restored once colchicine is removed? (answer should include information to explain both the ER & Golgi)
An integral membrane protein has an ER signal sequence near its N terminus and a stop transfer sequence in the middle. If a mutation removed the stop-transfer sequence, where would you expect to find the protein? Why?
The following image is based on real results from an influential experiment in cell biology. This experiment studied the role of the proteins Ran and importin in nuclear protein transport. The experiment used flourescently-labeled proteins containing a nuclear localization sequence (the "substrate"). Ran, importin, and GTP were either present or absent, as indicated in the figure. Cells were exposed to these different conditions and then analyzed by fluorescence microscopy. Circles are the cells' nuclei. Very light circles are the nuclei without the substrate attached. Study the figure below and then answer the questions that follow. 1. What actions does Ran perform by itself? 2. What actions does importin perform by itself? 3. How do Ran and importin act together in the nuclear import of protein? 4. Why is GTP required?
IN the figure for D: The organization of a protein that normally resides in the plasma membrane in shown in the figure below. The boxes labeled 1,2 3 and 4 represent membrane-spanning sequences and the arrow represents a site of action of signal peptidase. Given this diagram, which of the following statements must be true? (C) (D) oplasmic Reticulum The N-terminus of this protein is in the ER lumen The mature version of this protein will span the membrane twice, with both the N- and C-terminus in the cytoplasm. Two of the answers are correct The C-terminus of this protein is in the ER lumen
A 160 residue polytopic integral plasma membrane protein has the following sequence at its N-terminus. The amino terminal Ser is located inside the cytoplasm. Amino acids 11- 14 are localized outside the cell. N-¹Ser-Tyr-Leu-Gln-Ile-Arg-Phe-Asn-Leu-Lys-11 Gly-Pro-Gly-Ser-15 Glu-Phe-Gln-Leu-Asp- Ile-His-Leu-23 Ser-Gly-Gly Carefully analyze the sequence. (a) What do you predict for the overall tertiary structure of the entire 160 residue protein? (b) Give at least three reasons for your prediction. Ruling out alternatives, with proper logic, can count as a reason.
Consider the amino acids on the image below. Which of the following amino acids would be most likely to be found in the part of an integral membrane protein that is located within the membrane? (Select all answers that apply.) Asparagine (Asn) Lysine (Lys) Phenylalanine (Phe) Valine (Val) Glutamic acid (Glu) Methionine (Met)
Drawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (a) From the list below, select the amino acid(s) that might by more common in the extracellular domain of this membrane protein and whose side- chain can form hydrogen bonds with the surrounding water molecules. Explain why you selected this option(s). Lysine Serine Phenylalanine Methionine (b) From the list below, select the amino acid(s) that would likely be found in the transmembrane/ membrane spanning domain of this protein and whose side- chain interacts with the lipid bilayer. Lysine Serine Phenylalanine Methionine
Which of the following proteins is categorized as a multi-pass transmembrane protein (also called the anion exchange protein, because it exchanges chloride and bicarbonate ions in red blood cells)? band 3.0 protein (in the red blood cell membrane) COX-1 (in the lumenal leaflet of the smooth endoplasmic reticulum) glycophorin A (in the red blood cell membrane) the Ras protein (lipid-linked to the inner plasma membrane) cytochrome c (in the mitochondrion)
What is the significance of the protein-lined pits? O Protein attracts other proteins needed for ATP synthesis within the cell. Protein-lined pits are able to transport one molecule at a time down the concentration gradient within the cell. The polarity of proteins allows other polar molecules to attach and be transported in the cell by transport channels. Receptors within the pits allow ligands to fuse and be transported into the cell by endocytosis.
Proteins destined for which of the following destinations are transported through vesicles/the Endomembrane system? (i.e. not transported via post-translational import)
Phagocytosis of a bacterial cell by a macrophage, involves extensive remodeling of the actin microfilaments in the cell cortex to produce extensions of the plasma membrane and formation the phagocytic cup. Based on your knowledge of microfilament assembly/disassembly and related cell membrane deformation, explain the underlying processes that would be involved in formation of the phagocytic cup.
Integral membrane proteins are anchored in lipid bilayers. Which of the following groups of amino acid residues would likely be found in the portion that crosses the lipid bilayer? Nonpolar Polar Acidic Charged

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