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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Three mechanisms by which membrane-bind-ing proteins bend a membrane are illustrated in FigureQ10–2A, B, and C. As shown, each of these cytosolic mem-brane-bending proteins would induce an invagination ofthe plasma membrane. Could similar kinds of cytosolicproteins induce a protrusion of the plasma membrane(Figure Q10–2D)? Which ones? Explain how they mightwork.
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)?
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 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?
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 amino acid sequence Leu-His-Arg-Leu-Asp-Ala-Gln-SerLys-Leu-Ser-Ser is a signal sequence that directs proteinstowards the endoplasmic reticulum, say if it is true or false if it is false justify it.
What type of signal sequence(s) would be used to create the ACE2 (type 1) integral membrane protein?
If you were to remove the ER retrieval signal fromprotein disulfide isomerase (PDI), which is normally a sol-uble resident of the ER lumen, where would you expect themodified PDI to be located?
If the RGD tripeptide sequence in fibronevtin wete absent. Which is true? integrims would not bind to fibronectin cadherins on adjacent cells would not be able to interact in a homotypic fashion. fibronectin could not form crosslink with other extracellular matrix proteins. glycosaminoglycans would not be able to assemble onto proteoglycans.
REEP family proteins act as wedges to promote bending of the membrane true or false
Cytokine receptors and tyrosine kinase receptors are similar in all of the following ways EXCEPT one. Which one is the exception? O They are both down-regulated by lysosomal degradation They both involve receptor exoplasmic domain dimerization They both result in an effector protein entering the nucleus O They both involve cytosolic domain phosphorylation
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).

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