When scientists were first studying the fluidity of membranes, they did an experiment using hybrid cells. Certain membrane proteins in a human cell and a mouse cell were labeled using antibodies coupled with differently colored fluorescent tags. The two cells were then coaxed into fusing, resulting in the formation of a single, double-sized hybrid cell. Using fluorescence microscopy, the scientists then tracked the distribution of the labeled proteins in the hybrid cell. Which best describes the results they saw and what they ultimately concluded?
Choose one:
Initially, the mouse and human proteins were confined to their own halves of the newly formed hybrid cell, but over time, the two sets of proteins recombined such that they all fluoresced with a single, intermediate color.
Initially, the mouse and human proteins were confined to their own halves of the newly formed hybrid cell, but over time, the two sets of proteins became evenly intermixed over the entire cell surface. This suggests that proteins, like lipids, can move freely within the plane of the bilayer.
The mouse and human proteins began to intermix and spread across the surface of the hybrid cell, but over time, one set of proteins became dominant and the other set was lost.
This suggests that cells can ingest and destroy foreign proteins. At first, the mouse and human proteins were confined to their own halves of the newly formed hybrid cell, but over time, the two sets of proteins became divided such that half faced the cytosol and half faced the hybrid cell exterior.
This suggests that flippases are activated by cell fusion The mouse and human proteins remained confined to the portion of the plasma membrane that derived from their original cell type.
This suggests that cells can restrict the movement of their membrane proteins to establish cell-specific functional domains. Initially, the mouse and human proteins intermixed, but over time, they were able to resegregate into distinct membrane domains. This suggests that cells can restrict the movement of membrane proteins