If the pinsulin receptor, a, example of an integral membrane protein, is cotranslationally inserted into the ER membrane with the N-terminus on the cytosolicside of the membrane and the C-terminus in the lumen of the ER, which side of the receptor would you expect to bind to the ligand, pinsulin, when the it isfound on the cell surface?OlA. C-terminal end of the protein will bind pinsulinB. N-terminal end of the protein will bind pinsulinC. Neither will bind to a ligand because both ends of the protein will be cytoplasmicD. Neither will bind to a ligand because both ends of the protein will be extracellular and will compete with each other

The integral proteins are the proteins that are present usually in the plasma membrane or in the…

If the pinsulin receptor, a, example of an integral membrane protein, is cotranslationally inserted into the ER membrane with the N-terminus on the cytosolic side of the membrane and the č-terminus in the lumen of the ER, which side of the receptor would you expect to bind to the ligand, pinsulin, when the it is found on the cell surface? DA, C-terminal end of the protein will bind pinsulin O B. N-terminal end of the protein will bind pinsulin O. Neither will bind to a ligand because both ends of the protein will be cytoplasmic O D. Neither will bind to a ligand because both ends of the protein will be extracellular and will compete with each other

If the pinsulin receptor, a, example of an integral membrane protein, is cotranslationally inserted into the ER membrane with the N-terminus on the cytosolic side of the membrane and the č-terminus in the lumen of the ER, which side of the receptor would you expect to bind to the ligand, pinsulin, when the it is found on the cell surface? DA, C-terminal end of the protein will bind pinsulin O B. N-terminal end of the protein will bind pinsulin O. Neither will bind to a ligand because both ends of the protein will be cytoplasmic O D. Neither will bind to a ligand because both ends of the protein will be extracellular and will compete with each other

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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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.
When you think about the primary structure of the mannose-6-P receptor, assuming that it is an integral membrane protein with one membrane-spanning domain and assuming that it has a ERSS, what are all of the different protein domains that must be present in this protein's primary structure to get it to where it needs to go and to carry out all of the functions/activities? (Draw a schematic of the protein structure/sequence and explain each region). What do you think would happen to a soluble protein that normally contains a KDEL tag (ER retrieval) if the tag was cleaved off (where would the protein end up)?
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.
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
Where will the amino (NH2) terminus of the protein be located (cytosol vs. ER lumen) if the “start” signal is located at the amino terminus of the protein vs. the interior of the protein?
Histamine acts by binding to specialized membrane proteins called histamine H 1 receptors. These receptors, found in specific cells, are integral membrane proteins that possess seven transmembrane a-helical regions. The amino terminus of the protein is extracellular, while the C-terminus is cytoplasmic. The binding of histamine to the extracellular portion of the H 1 receptor prompts a conformational change in the intracellular C-terminus region of the protein. This conformational change triggers numerous intracellular signaling events that stimulate the immune response in cells containing the receptor. There are numerous anti-histamine drugs available commercially. Some of the most popular are shown here side by side with histamine: HCHS NH- Allegra H2N histamine Claritin Propose a reasonable mode of action by which these antihistamines exert their activity. Include relevant details about the system of your own choosing.
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?
Please use Transferrin receptor as an example of the protein whose pathway is being traced. If it is easier or possible, can there be a labeled drawing to explain.
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?
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.
The SRP receptor functions in the ER membrane. Which answer best describes its translation process and movement to destination for function?
8) Indicate which of the five major types of membrane protein (adhesion, enzymatic, recognition, receptor, and transport) is most likely to be involved in each of the situations described below: a) An oncologist wants to study the cells from a certain tumour that has been surgically removed from a patient. However, she must first treat the tumour with a solution affects a membrane protein on the tumour cells. Because of the effect of the solution on the membrane protein, the tumour tissue falls apart into individual cells. Type of membrane protein: b) Farmer Jebediah wakes up in the morning and makes himself an extra-strong coffee. The caffeine in the coffee attaches to a protein in the plasma membrane of his neurons, inducing a signal transduction cascade and causing Farmer Jebediah to be more alert Type of membrane protein: