Figure 8.
CAS transport kinetics reveals a distinct mechanism controlling its nuclear retention. (A) Successive image frames capture the photobleaching and fluorescence recovery of mCherry-CAS, mCherry-Δ40NCAS, and mCherry-CAS_T18D within the nucleus. Note: Only mCherry-CAS shows nuclear retention. Scale bar, 5 μm. (B) The gray value profile highlights the concentration gradient (i.e., slope) of mCherry-CAS that exists between the nucleus and cytoplasm but is absent in mCherry-Δ40NCAS and mCherry-CAS_T18D. (C) The recovery half-times for mCherry-CAS, mCherry-Δ40NCAS, mCherry-CAS_T18D, and mCherry-CAS_T18G are summarized in the boxplots for nuclear and cytoplasmic FRAP, respectively. Box plots denote the median, first, and third quartiles. The whiskers represent the minimum and maximum values. N = 3. The data were tested for normality using a built-in function of GraphPad Prism software. P values were obtained using an unpaired two-tailed t test.

CAS transport kinetics reveals a distinct mechanism controlling its nuclear retention. (A) Successive image frames capture the photobleaching and fluorescence recovery of mCherry-CAS, mCherry-Δ40NCAS, and mCherry-CAS_T18D within the nucleus. Note: Only mCherry-CAS shows nuclear retention. Scale bar, 5 μm. (B) The gray value profile highlights the concentration gradient (i.e., slope) of mCherry-CAS that exists between the nucleus and cytoplasm but is absent in mCherry-Δ40NCAS and mCherry-CAS_T18D. (C) The recovery half-times for mCherry-CAS, mCherry-Δ40NCAS, mCherry-CAS_T18D, and mCherry-CAS_T18G are summarized in the boxplots for nuclear and cytoplasmic FRAP, respectively. Box plots denote the median, first, and third quartiles. The whiskers represent the minimum and maximum values. N = 3. The data were tested for normality using a built-in function of GraphPad Prism software. P values were obtained using an unpaired two-tailed t test.

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