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Figure 3.
Figure 3: Inhibition of the Yap1 NES by the n- alpha- 1
helix. a, Ribbon diagram of the Yap1-RD structure with the
lowest energy shown in the same orientation as Fig. 2c. The n-
 1
helix and the regions of c-CRD secondary structure are shown in
cyan and dark blue, respectively. The NES residues Ile614,
Val616, Leu619 and Leu623 are shown in green. These interact
with other hydrophobic core residues of the c-CRD, which are
shown in grey. b, The same ribbon diagram as in Fig. 3a, rotated
to show the n- 1
residues. The amphipathic n- 1
helix contains conserved hydrophobic residues, Phe302, Met306
and Val309, shown in red. c, Surface representation of the c-CRD
domain and its interaction with the hydrophobic residues in the
n- 1
helix. The surface of the NES residues Ile614, Val616, Leu619
and Leu623 are shown in green and Phe302, Met306 and Val309 in
red. d, Fluorescence microscopy of cells expressing Yap1-RD^GFP
F302A, M306A and V309A mutants, untreated or treated with
H[2]O[2] as carried out in Fig. 1b. e, Oxidized and reduced
Yap1-RD^GFP F302A, M306A and V309A mutants extracted from
exponentially growing cells untreated or treated with H[2]O[2].
The cell extracts were prepared as in Fig. 1c.
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