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.

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.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter9: Cell Communication

Section: Chapter Questions

Problem 3ITD

See similar textbooks

Similar questions

Focal adhesion complex attachment to extracellular matrix molecules is mediated by: heterodimers of alpha-integrin and beta integrin homodimers of classical cafherins The force of gravity actin filaments
What will happen if Sec23/24 has a mutation that stops it from attaching to cargo receptors? Consider how this would effect the coat's construction, vesicle formation, and overall vesicle transport between two membrane compartments including the vesicles generated by this protein coat.
REEP family proteins act as wedges to promote bending of the membrane true or false
What integral membrane protein family made of two membrane-spanning chains (α and β) is involved in attaching cells to their extracellular microenvironment? a) lamininsb) fibronectinsc) integrinsd) myosinse) lysins
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.
As we age our skin becomes thin and easily tears. One potential reason to explain would be if adjacent cells within the skin lose the ability to attach to each other strongly. Another reason could be that cells lose the ability to attach strongly to the extracellular matrix. Compare and contrast these membrane functions and suggest which proteins might be “lost” as we age to cause the loss of attachment function in each scenario
All are protiens of cell membrane that are involved in flow of nerve impulse except 1-channel proteins 2-carrier protiens 3-peripheral protiens 4-integral protiens Also give explanation
Various types of vesicle coats have been implicated in membrane traffic pathways suchas endocytosis, export from the ER to the Golgi, and transport between Golgicisternae. But so far, no coat has been identified for the secretory vesicles that carrymaterial from the Golgi to the plasma membrane. Do you think such a coat is likely toexist? Justify your answer.
When the protein integrin (a transmembrane protein in human fibroblasts) is held in place, by covalent bonds to fibronectin and collagen proteins in the interstitial spaces, integrin is exhibiting: restricted movement in the membrane, based on confinement by diffusion barriers restricted movement in the membrane, based on tethering to extracellular molecules restricted movement in the membrane, based on attachment to other cells restricted movement in the membrane, based on anchoring to intracellular proteins unrestricted movement in the membrane, similar to membrane lipids
What are the basic properties of e-cadherins? Namely, what is the basic structure of specifically e-cadherins, what affects their function (e.g. Ca2+), their ligand activity, and their role in cell sorting? Be specific/distinct with every point here.
Although purified actin can assemble reversibly in vitro, various actin-binding proteins regulate the assembly of actin filaments in the cell. Predict the effect on a cell’s actin cytoskeleton if function-blocking antibodies against each of the following were independently microinjected into cells: profilin, thymosin-β4, CapZ, and the Arp2/3 complex.
Transmembrane portrudes on both sides. Integral protein is in the width of the bilayer and may portrude on one or both sides of the bilayer. Is Transmembrane Protein semi-similar to Integral Proteins? How can we tell the difference of the two?