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Characterization of EHop-016, Novel Small Molecule Inhibitor of Rac GTPase

Montalvo-Ortiz, Brenda L., Castillo-Pichardo, Linette, Hernández, Eliud, Humphries-Bickley, Tessa, De La Mota-Peynado, Alina, Cubano, Luis A., Vlaar, Cornelis P., Dharmawardhane, Suranganie·2012·Journal of Biological Chemistry
DOI 10.1074/jbc.m111.334524
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CC-BY · From the PDF
FIGURE1 SynthesisanddockingofEHop-016intotheputativeGEFbindingpocketofRac1. A , synthetic scheme for the preparation of EHop-016. The synthesis was performed by a two-step approach as described (57). B , EHop016 docked into the GEF binding pocket of Rac1 and its comparison with the position of NSC23766 in the crystal structure of the Rac1-NSC23766 complex.
FIGURE1 SynthesisanddockingofEHop-016intotheputativeGEFbindingpocketofRac1. A , synthetic scheme for the preparation of EHop-016. The synthesis was performed by a two-step approach as described (57). B , EHop016 docked into the GEF binding pocket of Rac1 and its comparison with the position of NSC23766 in the crystal structure of the Rac1-NSC23766 complex.CC-BY · From the PDF
FIGURE 2 Effect of EHop-016 and NSC23766 on Rac activity. MDA-MB-435 cells were treated with vehicle (0.1% DMSO) or varying concentrations of EHop-016 (0-10 𝛍 M) or NSC23766 (0-100 𝛍 M) for 24 h. Cell lysates were subjected to the G-LISA Rac1 activation assay (Cytoskeleton, Inc.). IC 50 curves for percentage Rac activity are relative to vehicle from three biological replicates each with two technical replicates. Error bars , S.D. Four-parameter dose-response curves generated using GraphPad Prism H23006 are shown.
FIGURE 2 Effect of EHop-016 and NSC23766 on Rac activity. MDA-MB-435 cells were treated with vehicle (0.1% DMSO) or varying concentrations of EHop-016 (0-10 𝛍 M) or NSC23766 (0-100 𝛍 M) for 24 h. Cell lysates were subjected to the G-LISA Rac1 activation assay (Cytoskeleton, Inc.). IC 50 curves for percentage Rac activity are relative to vehicle from three biological replicates each with two technical replicates. Error bars , S.D. Four-parameter dose-response curves generated using GraphPad Prism H23006 are shown.CC-BY · From the PDF
FIGURE3 EffectofEHop-016onRhoGTPaseactivity. A and B , MDA-MB-435 cells were treated with vehicle (0) or EHop-016 at the indicated concentrations (1, 2, 4, 5, or 10 𝛍 M) for 24 h. Cell lysates were subjected to a pull-down assay using a GST-CRIB domain of PAK and Western blotted for Rac3 or Cdc42. C , a GST-RBD domain of rhotekin was used to pull down Rho-GTP and detected by Western blotting with anti-RhoA antibody. The average percentage of Rho GTPase activity was calculated from the integrated density of positive bands of Rho GTPase-GTP from a pull-down/total Rho GTPase in cell lysate for each treatment and each Rho GTPase (Rac3, Cdc42, or RhoA) relative to vehicle controls. A , representative Western blot of pull-downs immunostained for Rac3-GTP ( top row ) or total Rac3 in cell lysate ( bottom row ) ( n = 3). B , representative Western blots (from the same experiment) of pull-downs immunostained for Cdc42-GTP ( top row ) or total Cdc42 in cell lysate ( bottom row ) ( n = 2). C , representative Western blots of pull-downs immunostained for RhoA-GTP( toprow ) or total RhoA in cell lysate ( bottomrow ), n = 3. Western blots show positive bands for Rho GTPases at ∼ 21 kDa.
FIGURE3 EffectofEHop-016onRhoGTPaseactivity. A and B , MDA-MB-435 cells were treated with vehicle (0) or EHop-016 at the indicated concentrations (1, 2, 4, 5, or 10 𝛍 M) for 24 h. Cell lysates were subjected to a pull-down assay using a GST-CRIB domain of PAK and Western blotted for Rac3 or Cdc42. C , a GST-RBD domain of rhotekin was used to pull down Rho-GTP and detected by Western blotting with anti-RhoA antibody. The average percentage of Rho GTPase activity was calculated from the integrated density of positive bands of Rho GTPase-GTP from a pull-down/total Rho GTPase in cell lysate for each treatment and each Rho GTPase (Rac3, Cdc42, or RhoA) relative to vehicle controls. A , representative Western blot of pull-downs immunostained for Rac3-GTP ( top row ) or total Rac3 in cell lysate ( bottom row ) ( n = 3). B , representative Western blots (from the same experiment) of pull-downs immunostained for Cdc42-GTP ( top row ) or total Cdc42 in cell lysate ( bottom row ) ( n = 2). C , representative Western blots of pull-downs immunostained for RhoA-GTP( toprow ) or total RhoA in cell lysate ( bottomrow ), n = 3. Western blots show positive bands for Rho GTPases at ∼ 21 kDa.CC-BY · From the PDF
FIGURE 4 Effect of EHop-016 on Rac/Rac GEF interaction. MDA-MB-435cells were lysed and incubated with glutathione-agarose-coupled GST-Rac1(G15A) beadstopull down activated Rac GEFs. A , a representative Western blot (from the same experiment) of GST-Rac1(G15A) pull-down, supernatant ( sup ) from the incubation, and cell lysates, immunostained for Trio, Tiam-1, or Vav2. B , GST-Rac1(G15A) beads were preincubated with vehicle (0), or 2 or 4 𝛍 MEHop-016prior to incubation with MDA-MB-435 cell lysates. A representative Western blot (from the same experiment) ( n = 3) immunostained for Vav2 is shown. Top row , pull-down; bottom row , total cell lysate. C , quantification of the percentage of average Vav2 (two bands at ∼ 100 kDa) associated with the Rac1(G15A) beads frompull-downassaysinthepresenceorabsenceofEHop-016.ImageJsoftwarewasusedtoquantifytheintegrateddensityofpositivebands( ∼ 100kDa)from Vav2 Western blots of pull-downs. Data are represented relative to vehicle controls (100%). D and E , purified His-tagged Tiam-1 DH/PH domain was added at a concentration of 2:1 to Rac1(G15A) beads that were preincubated with vehicle ( Veh ) or Ehop-016 or NSC23766 at the indicated concentrations for 1 h at 4 °C. Pull-downs were washed and immunoblotted with an anti-His antibody to detect His-Tiam-1 as a ∼ 45 kDa band. D , a representative Western blot (from the same experiment). Top , GST-Rac1(G15A) pull-downs; bottom , supernatants. E , quantification of percentage of Tiam-1 (DH/PH) domain associated with Rac1(G15A) beads in the presence or absence of EHop-016 or NSC23766. n = 3. Error bars , S.D. *, statistical significance compared with vehicle controls ( p ≤ 0.05).
FIGURE 4 Effect of EHop-016 on Rac/Rac GEF interaction. MDA-MB-435cells were lysed and incubated with glutathione-agarose-coupled GST-Rac1(G15A) beadstopull down activated Rac GEFs. A , a representative Western blot (from the same experiment) of GST-Rac1(G15A) pull-down, supernatant ( sup ) from the incubation, and cell lysates, immunostained for Trio, Tiam-1, or Vav2. B , GST-Rac1(G15A) beads were preincubated with vehicle (0), or 2 or 4 𝛍 MEHop-016prior to incubation with MDA-MB-435 cell lysates. A representative Western blot (from the same experiment) ( n = 3) immunostained for Vav2 is shown. Top row , pull-down; bottom row , total cell lysate. C , quantification of the percentage of average Vav2 (two bands at ∼ 100 kDa) associated with the Rac1(G15A) beads frompull-downassaysinthepresenceorabsenceofEHop-016.ImageJsoftwarewasusedtoquantifytheintegrateddensityofpositivebands( ∼ 100kDa)from Vav2 Western blots of pull-downs. Data are represented relative to vehicle controls (100%). D and E , purified His-tagged Tiam-1 DH/PH domain was added at a concentration of 2:1 to Rac1(G15A) beads that were preincubated with vehicle ( Veh ) or Ehop-016 or NSC23766 at the indicated concentrations for 1 h at 4 °C. Pull-downs were washed and immunoblotted with an anti-His antibody to detect His-Tiam-1 as a ∼ 45 kDa band. D , a representative Western blot (from the same experiment). Top , GST-Rac1(G15A) pull-downs; bottom , supernatants. E , quantification of percentage of Tiam-1 (DH/PH) domain associated with Rac1(G15A) beads in the presence or absence of EHop-016 or NSC23766. n = 3. Error bars , S.D. *, statistical significance compared with vehicle controls ( p ≤ 0.05).CC-BY · From the PDF
FIGURE5 Effect of EHop-016onRacactivityandtheactincytoskeletonofmetastaticcancercells. A , MDA-MB-231orMDA-MB-435cellsweretreatedwith vehicle (0) or EHop-016 at the indicated concentrations (2 or 4 𝛍 M) for 24 h. Cell lysates were subjected to a pull-down assay using a GST-CRIB domain of PAK andWesternblotted for Rac (Rac1, -2, and -3). Representative Western blot (from the same experiment) of pull-downs immunostained for Rac-GTP ( top row ) or total Rac in cell lysate ( bottomrow ). n = 3. B , MDA-MB-231 or MDA-MB-435 metastatic breast cancer cells were treated with vehicle or EHop-016 at 2 or 4 𝛍 Mfor 24 h to determine changes in actin cytoskeletal structures. Cells were fixed, permeabilized, and stained with rhodamine phalloidin to visualize F-actin. Top , representative micrographs are shown at × 600 magnification. Arrows , lamellipodia; arrowheads , filopodia. Bottom , percentage of cells that demonstrated lamellipodia was quantified for each treatment from 10 representative microscopic fields. Error bars , S.E. *, statistical significance compared with vehicle controls ( p ≤ 0.001).
FIGURE5 Effect of EHop-016onRacactivityandtheactincytoskeletonofmetastaticcancercells. A , MDA-MB-231orMDA-MB-435cellsweretreatedwith vehicle (0) or EHop-016 at the indicated concentrations (2 or 4 𝛍 M) for 24 h. Cell lysates were subjected to a pull-down assay using a GST-CRIB domain of PAK andWesternblotted for Rac (Rac1, -2, and -3). Representative Western blot (from the same experiment) of pull-downs immunostained for Rac-GTP ( top row ) or total Rac in cell lysate ( bottomrow ). n = 3. B , MDA-MB-231 or MDA-MB-435 metastatic breast cancer cells were treated with vehicle or EHop-016 at 2 or 4 𝛍 Mfor 24 h to determine changes in actin cytoskeletal structures. Cells were fixed, permeabilized, and stained with rhodamine phalloidin to visualize F-actin. Top , representative micrographs are shown at × 600 magnification. Arrows , lamellipodia; arrowheads , filopodia. Bottom , percentage of cells that demonstrated lamellipodia was quantified for each treatment from 10 representative microscopic fields. Error bars , S.E. *, statistical significance compared with vehicle controls ( p ≤ 0.001).CC-BY · From the PDF
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CC-BY · From the PDF
Image 8
CC-BY · From the PDF

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Cited by

Metadata

Authors
Montalvo-Ortiz, B. L., Castillo-Pichardo, L., Hernández, E., Humphries-Bickley, T., De La Mota-Peynado, A., Cubano, L. A., Vlaar, C. P., & Dharmawardhane, S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2012-04
Volume
287
Issue
16
Pages
13228-13238
ISSN
0021-9258
DOI
10.1074/jbc.m111.334524
Cited by
213
References
7
Language
en
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