As opposed to clathrin vesicles, COP1 vesicles DO NOT bud by a GTP-independent process retrograde transport from the Golgi to the ER More than one answer mediate retrograde transport from the cis-Golgi to the trans Golgi contain a receptor that recognizes mannose-6-phosphate
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- 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.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.You are studying the binding of proteins to thecytoplasmic face of cultured neuroblastoma cells andhave found a method that gives a good yield of inside-outvesicles from the plasma membrane. Unfortunately, yourpreparations are contaminated with variable amounts ofright-side-out vesicles. Nothing you have tried avoids thisproblem. A friend suggests that you pass your vesicles overan affinity column made of lectin coupled to solid beads.What is the point of your friend’s suggestion?
- The enzymes GICNAC phosphotrasnferase is a key enzyme involved in the transporting of proteins from the trans-Golgi to the lysozyme. In addition to the catalytic function of the enzyme that involves certain sugars, what is the second critical function of this enzyme? O It recognizes internal signal sequences found on lysozyme-targeted proteins. O It drives the binding of a phosphorylated GlcNac group onto a mannose residue. O It facilitates the reversible binding of specific proteins to the M6P receptor O In is essential for the recruitment of clathrin triskelions to the budding vesicle.Mutations in the nuclear laminproteins cause a large number ofdiseases called laminopathies. What dowe not understand about the nuclearlamina that could account for this fact?REEP family proteins act as wedges to promote bending of the membrane true or false
- 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?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
- 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.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.It is not an easy matter to assign particular func-tions to specific components of the basal lamina, sincethe overall structure is a complicated composite materialwith both mechanical and signaling properties. Nidogen,for example, cross-links two central components of thebasal lamina by binding to the laminin γ-1 chain and totype IV collagen. Given such a key role, it was surprisingthat mice with a homozygous knockout of the gene fornidogen-1 were entirely healthy, with no abnormal phe-notype. Similarly, mice homozygous for a knockout of thegene for nidogen-2 also appeared completely normal. Bycontrast, mice that were homozygous for a defined muta-tion in the gene for laminin γ-1, which eliminated just thebinding site for nidogen, died at birth with severe defectsin lung and kidney formation. The mutant portion of thelaminin γ-1 chain is thought to have no other functionthan to bind nidogen, and does not affect laminin struc-ture or its ability to assemble into the basal lamina.…