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The C-Terminal Sequence of RhoB Directs Protein Degradation through an Endo-Lysosomal Pathway

Pérez-Sala, Dolores, Boya, Patricia, Ramos, Irene, Herrera, Mónica, Stamatakis, Konstantinos·2009·PLoS ONE
DOI 10.1371/journal.pone.0008117PMC PMC2780327
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Figure 1 RhoB is degraded through a lysosomal pathway. (a) Confluent serum-deprived bovine aortic endothelial cells (BAEC) were treated with 10 µM lactacystin, 50 nM Z-LLL-CHO, 10 µM ALLM, 50 µg/ml leupeptin or 10 µM chloroquine for 24 h. Cell lysates (20 µg of protein) were analyzed by Western blot. RhoB and ubiquitinated protein levels corrected by RhoGDI levels are shown as average values ± SEM of three experiments (*p<0.05 vs control). (b) BAEC were pre-treated with the inhibitors for 30 min. NH4Cl and bafilomycin A1 were added at 30 mM and 5 nM, final concentrations, respectively. RhoB levels were assessed before and after treatment with CHX (20 µg/ml). Levels of RhoGDI were used as control. The percentage of RhoB remaining after 3 h CHX treatment is shown as average values ± SEM of at least three different experiments (*p<0.05 vs control). (c) BAEC were treated with 50 µg/ml leupeptin plus 5 µg/ml E64d or 10 µM chloroquine for 24 h and visualized by immunofluorescence (IF) of endogenous RhoB (green) and staining with 500 nM LTR (red) and DAPI (blue). Images shown are single confocal sections. Bar, 20 µm. (d) BAEC were treated with 30 mM NH4Cl or 5 nM bafilomycin A1 for 24 h and fixed. Nuclei were stained with DAPI (blue) and RhoB (green) was detected by IF and confocal microscopy. Images are shown as maximal projections of confocal planes of 0.5 µm Z-sections. Bar, 20 µm. (e) BAEC subjected to osmotic shock for 5 min were allowed to recover in the absence or presence of 10 mM potassium chloride (K+) for 3 h, during which CHX (20 µg/ml) was present to block new protein synthesis. RhoB levels were assessed by Western blot.
Figure 1 RhoB is degraded through a lysosomal pathway. (a) Confluent serum-deprived bovine aortic endothelial cells (BAEC) were treated with 10 µM lactacystin, 50 nM Z-LLL-CHO, 10 µM ALLM, 50 µg/ml leupeptin or 10 µM chloroquine for 24 h. Cell lysates (20 µg of protein) were analyzed by Western blot. RhoB and ubiquitinated protein levels corrected by RhoGDI levels are shown as average values ± SEM of three experiments (*p<0.05 vs control). (b) BAEC were pre-treated with the inhibitors for 30 min. NH4Cl and bafilomycin A1 were added at 30 mM and 5 nM, final concentrations, respectively. RhoB levels were assessed before and after treatment with CHX (20 µg/ml). Levels of RhoGDI were used as control. The percentage of RhoB remaining after 3 h CHX treatment is shown as average values ± SEM of at least three different experiments (*p<0.05 vs control). (c) BAEC were treated with 50 µg/ml leupeptin plus 5 µg/ml E64d or 10 µM chloroquine for 24 h and visualized by immunofluorescence (IF) of endogenous RhoB (green) and staining with 500 nM LTR (red) and DAPI (blue). Images shown are single confocal sections. Bar, 20 µm. (d) BAEC were treated with 30 mM NH4Cl or 5 nM bafilomycin A1 for 24 h and fixed. Nuclei were stained with DAPI (blue) and RhoB (green) was detected by IF and confocal microscopy. Images are shown as maximal projections of confocal planes of 0.5 µm Z-sections. Bar, 20 µm. (e) BAEC subjected to osmotic shock for 5 min were allowed to recover in the absence or presence of 10 mM potassium chloride (K+) for 3 h, during which CHX (20 µg/ml) was present to block new protein synthesis. RhoB levels were assessed by Western blot.CC BY · PubMed Central
Figure 2 Localization of RhoB along the endo-lysosomal pathway. (a) BAEC transiently transfected with GFP-RhoB were incubated with Texas Red-labeled dextran (Dextran-TXR) for 5 min and visualized by confocal microscopy after 1 h. Bar, 20 µm. (b) BAEC were transiently transfected with the indicated constructs and 24 h later live cells were observed by confocal microscopy. Bars, 15 µm. (c) BAEC were transfected with GFP-RhoB, RFP-RhoB and/or Lamp1-GFP and treated 24 h later with leupeptin plus E64d or chloroquine for further 24 h. When indicated, cells were incubated with 25 nM LTR for 15 min. Live cells were observed by confocal microscopy. Bars, 15 µm. (d) Transmission EM of MVB from control and chloroquine treated BAEC. Bars, 1 µm. (e) IEM analysis of GFP-RhoB in control and choroquine-treated cells by staining with anti-GFP antibody. Bars, 1 µm.
Figure 2 Localization of RhoB along the endo-lysosomal pathway. (a) BAEC transiently transfected with GFP-RhoB were incubated with Texas Red-labeled dextran (Dextran-TXR) for 5 min and visualized by confocal microscopy after 1 h. Bar, 20 µm. (b) BAEC were transiently transfected with the indicated constructs and 24 h later live cells were observed by confocal microscopy. Bars, 15 µm. (c) BAEC were transfected with GFP-RhoB, RFP-RhoB and/or Lamp1-GFP and treated 24 h later with leupeptin plus E64d or chloroquine for further 24 h. When indicated, cells were incubated with 25 nM LTR for 15 min. Live cells were observed by confocal microscopy. Bars, 15 µm. (d) Transmission EM of MVB from control and chloroquine treated BAEC. Bars, 1 µm. (e) IEM analysis of GFP-RhoB in control and choroquine-treated cells by staining with anti-GFP antibody. Bars, 1 µm.CC BY · PubMed Central
Figure 3 Effect of endosomal lipid dynamics on RhoB distribution. (a) BAEC were treated with vehicle or 10 µM U18666A for 24 h, fixed and analyzed by transmission EM. Bars, 1 µm. (b) Confocal microscopy GFP-RhoB-transfected cells treated as in A. DIC, fluorescent image and their overlay are shown. Bars, 20 µm. (c) BAEC were transfected with the indicated constructs and treated with vehicle or U18666A; (a,b) and (e,f), confocal microscopy of live cells incubated with 25 nM LTR; cell contours are shown by dotted lines in (e,f); (c,d) distribution of LBPA observed by IF. Nuclei were stained with DAPI. Bars, 10 µm. (d) The degree of internalization of GFP-RhoB or GFP-Rab7 into U18666A-induced structures was estimated from co-localization of the corresponding constructs with LTR and it is shown as average values ± SEM from three independent experiments (*p<0.05 vs control). (e) BAEC transfected with GFP-RhoB and treated with U18666A were analyzed by IEM with anti-GFP antibodies. Bar, 0.5 µm. (f) Effect of anti-LBPA on RhoB distribution. BAEC transfected with GFP-RhoB were incubated with a control antibody or with anti-LBPA (hybridoma supernatant diluted 1∶1 in culture medium) for 20 h; (a,b) live cells observed by confocal microscopy; (c,d) accumulation of LBPA observed by IF with anti-mouse Ig antibody. Bars, 20 µm. (g) Control or NPC fibroblasts were transfected with GFP-RhoB. Co-localization with LTR was assessed in live cells. Bars, 20 µm. Co-localization is shown as average values ± SEM of determinations from three experiments (*p<0.05 vs control).
Figure 3 Effect of endosomal lipid dynamics on RhoB distribution. (a) BAEC were treated with vehicle or 10 µM U18666A for 24 h, fixed and analyzed by transmission EM. Bars, 1 µm. (b) Confocal microscopy GFP-RhoB-transfected cells treated as in A. DIC, fluorescent image and their overlay are shown. Bars, 20 µm. (c) BAEC were transfected with the indicated constructs and treated with vehicle or U18666A; (a,b) and (e,f), confocal microscopy of live cells incubated with 25 nM LTR; cell contours are shown by dotted lines in (e,f); (c,d) distribution of LBPA observed by IF. Nuclei were stained with DAPI. Bars, 10 µm. (d) The degree of internalization of GFP-RhoB or GFP-Rab7 into U18666A-induced structures was estimated from co-localization of the corresponding constructs with LTR and it is shown as average values ± SEM from three independent experiments (*p<0.05 vs control). (e) BAEC transfected with GFP-RhoB and treated with U18666A were analyzed by IEM with anti-GFP antibodies. Bar, 0.5 µm. (f) Effect of anti-LBPA on RhoB distribution. BAEC transfected with GFP-RhoB were incubated with a control antibody or with anti-LBPA (hybridoma supernatant diluted 1∶1 in culture medium) for 20 h; (a,b) live cells observed by confocal microscopy; (c,d) accumulation of LBPA observed by IF with anti-mouse Ig antibody. Bars, 20 µm. (g) Control or NPC fibroblasts were transfected with GFP-RhoB. Co-localization with LTR was assessed in live cells. Bars, 20 µm. Co-localization is shown as average values ± SEM of determinations from three experiments (*p<0.05 vs control).CC BY · PubMed Central
Figure 4 Effect of Vps4 wt and DN on RhoB localization and stability. (a–b) BAEC were transfected with GFP-Vps4 wt or DN, as indicated, and 24 h later, treated in the absence or presence of 10 µM chloroquine for 24 h. In (b), 25 nM LTR was added 15 min before observation of live cells by confocal microscopy. Bars, 15 µm. (c) BAEC were transfected as above and 24 later placed in serum-free medium. After 24 h, control (0 time, -) cells were fixed, and the rest were treated with 20 µg/ml CHX for 8 h (+) to allow degradation of endogenous RhoB, before fixation. Endogenous RhoB (in red) was detected by IF. Nuclei were stained with DAPI. Images shown are overall projections. Bars, 20 µm. The lower panel shows the proportion of RhoB-positive cells among non-transfected (NT) cells or among cells transfected with the indicated constructs before (−) or after CHX (+) treatment. At least 40 cells of each type were monitored from four independent experiments. Results are shown as average values ± SEM (*p<0.05 vs the same condition in the absence of CHX). (d) COS7 cells were transfected with GFP-Vps4 wt or DN, as indicated, and 24 h later split in three dishes for treatment with CHX for the indicated times. RhoB and RhoGDI levels were assessed by Western blot. Results shown are average values ± SEM from three experiments (*p<0.05 vs GFP-Vps4 DN at the same time points).
Figure 4 Effect of Vps4 wt and DN on RhoB localization and stability. (a–b) BAEC were transfected with GFP-Vps4 wt or DN, as indicated, and 24 h later, treated in the absence or presence of 10 µM chloroquine for 24 h. In (b), 25 nM LTR was added 15 min before observation of live cells by confocal microscopy. Bars, 15 µm. (c) BAEC were transfected as above and 24 later placed in serum-free medium. After 24 h, control (0 time, -) cells were fixed, and the rest were treated with 20 µg/ml CHX for 8 h (+) to allow degradation of endogenous RhoB, before fixation. Endogenous RhoB (in red) was detected by IF. Nuclei were stained with DAPI. Images shown are overall projections. Bars, 20 µm. The lower panel shows the proportion of RhoB-positive cells among non-transfected (NT) cells or among cells transfected with the indicated constructs before (−) or after CHX (+) treatment. At least 40 cells of each type were monitored from four independent experiments. Results are shown as average values ± SEM (*p<0.05 vs the same condition in the absence of CHX). (d) COS7 cells were transfected with GFP-Vps4 wt or DN, as indicated, and 24 h later split in three dishes for treatment with CHX for the indicated times. RhoB and RhoGDI levels were assessed by Western blot. Results shown are average values ± SEM from three experiments (*p<0.05 vs GFP-Vps4 DN at the same time points).CC BY · PubMed Central
Figure 5 Structural determinants involved in the subcellular localization and degradation of GFP-RhoB. (a,b) NIH-3T3 fibroblasts were transiently transfected with the indicated GFP constructs. 24 h after transfection, the distribution of fluorescent constructs was assessed by confocal microscopy of live cells. Bars, 20 µm. The putative posttranslational modifications of each construct are shown schematically above the panels. Construct stability was assessed by blocking protein synthesis with CHX and estimating the remaining levels by Western blot with anti-GFP antibody. Blots show the levels of the constructs of interest and of RhoGDI, as control. Lower panels show the construct levels remaining after 6 h treatment with CHX. wt, GFP-RhoB; C193S, GFP-RhoB C193S; C189S, GFP-RhoB C189S; C192S, GFP-RhoB C192S; C189,192S, GFP-RhoB C189,192S; RhoA, GFP-RhoA. Results are shown as average values ± SEM of three different experiments (*p<0.05 vs wt levels in (a) and vs GFP-4 levels in (b)).
Figure 5 Structural determinants involved in the subcellular localization and degradation of GFP-RhoB. (a,b) NIH-3T3 fibroblasts were transiently transfected with the indicated GFP constructs. 24 h after transfection, the distribution of fluorescent constructs was assessed by confocal microscopy of live cells. Bars, 20 µm. The putative posttranslational modifications of each construct are shown schematically above the panels. Construct stability was assessed by blocking protein synthesis with CHX and estimating the remaining levels by Western blot with anti-GFP antibody. Blots show the levels of the constructs of interest and of RhoGDI, as control. Lower panels show the construct levels remaining after 6 h treatment with CHX. wt, GFP-RhoB; C193S, GFP-RhoB C193S; C189S, GFP-RhoB C189S; C192S, GFP-RhoB C192S; C189,192S, GFP-RhoB C189,192S; RhoA, GFP-RhoA. Results are shown as average values ± SEM of three different experiments (*p<0.05 vs wt levels in (a) and vs GFP-4 levels in (b)).CC BY · PubMed Central
Figure 6 Localization of GFP-CINCCKVL in endo-lysosomal compartments. (a) BAEC transfected with RFP-RhoB and/or GFP-CINCCKVL (GFP-8) were treated with vehicle, 10 µM chloroquine or 5 nM bafilomycin A1, incubated with 25 nM LTR when indicated and visualized live by confocal microscopy. (b) BAEC transfected with GFP-8 were treated with 10 µM U18666A for 24 h. DIC and fluorescence images showing dense lysosomes and GFP-8 accumulations are shown. (c) BAEC transfected with GFP-8 and RFP-RhoB and treated with U18666A as above were fixed and co-localization of GFP-8, RFP-RhoB and LBPA was detected by IF. Bars, 20 µm.
Figure 6 Localization of GFP-CINCCKVL in endo-lysosomal compartments. (a) BAEC transfected with RFP-RhoB and/or GFP-CINCCKVL (GFP-8) were treated with vehicle, 10 µM chloroquine or 5 nM bafilomycin A1, incubated with 25 nM LTR when indicated and visualized live by confocal microscopy. (b) BAEC transfected with GFP-8 were treated with 10 µM U18666A for 24 h. DIC and fluorescence images showing dense lysosomes and GFP-8 accumulations are shown. (c) BAEC transfected with GFP-8 and RFP-RhoB and treated with U18666A as above were fixed and co-localization of GFP-8, RFP-RhoB and LBPA was detected by IF. Bars, 20 µm.CC BY · PubMed Central
Figure 7 Subcellular localization and stability of chimeric proteins bearing -CINCCKVL C-terminal sequences. (a) BAEC were co-transfected with tagRFP or tagRFP-CINCCKVL (tagRFP-8) and GFP-RhoB or Lamp1-GFP, as indicated, treated for 24 h in the absence or presence of 10 µM chloroquine and directly visualized by confocal microscopy. Images shown are individual confocal sections. Bars, 20 µm. (b) The stability of tagRFP and tagRFP-8 was assessed in BAEC as described in Fig. 5, using an anti-tagRFP antibody. Results are shown as average values ± SD of at least three determinations (*p<0.05 vs tagRFP levels at the same time points). (c) BAEC were transfected with GFP-RhoGDI, GFP-RhoGDI-8 and/or RFP-RhoB, incubated with 25 nM LTR, as indicated, and directly observed by confocal microscopy. Bar, 20 µm. (d) BAEC were transfected with GFP-RhoGDI-8 in the absence (a) or presence (c) of 10 µM simvastatin. 24 h after transfection, confocal images of live cells were obtained (a, c). At that point, simvastatin was withdrawn from (c) and added to (a). After a 24 h additional incubation images of live cells were taken (b, d). Bar, 20 µm. (e,f) BAEC were transiently transfected with GFP-RhoGDI-8 or GFP-RhoGDI. In (e) protein synthesis was blocked by CHX addition. In (f) BAEC were treated with the indicated agents for 24 h. Levels of GFP-RhoGDI-8, GFP-RhoGDI and endogenous RhoGDI, were assessed by Western blot. Sv, simvastatin; Chlo, chloroquine; Leu, leupeptin.
Figure 7 Subcellular localization and stability of chimeric proteins bearing -CINCCKVL C-terminal sequences. (a) BAEC were co-transfected with tagRFP or tagRFP-CINCCKVL (tagRFP-8) and GFP-RhoB or Lamp1-GFP, as indicated, treated for 24 h in the absence or presence of 10 µM chloroquine and directly visualized by confocal microscopy. Images shown are individual confocal sections. Bars, 20 µm. (b) The stability of tagRFP and tagRFP-8 was assessed in BAEC as described in Fig. 5, using an anti-tagRFP antibody. Results are shown as average values ± SD of at least three determinations (*p<0.05 vs tagRFP levels at the same time points). (c) BAEC were transfected with GFP-RhoGDI, GFP-RhoGDI-8 and/or RFP-RhoB, incubated with 25 nM LTR, as indicated, and directly observed by confocal microscopy. Bar, 20 µm. (d) BAEC were transfected with GFP-RhoGDI-8 in the absence (a) or presence (c) of 10 µM simvastatin. 24 h after transfection, confocal images of live cells were obtained (a, c). At that point, simvastatin was withdrawn from (c) and added to (a). After a 24 h additional incubation images of live cells were taken (b, d). Bar, 20 µm. (e,f) BAEC were transiently transfected with GFP-RhoGDI-8 or GFP-RhoGDI. In (e) protein synthesis was blocked by CHX addition. In (f) BAEC were treated with the indicated agents for 24 h. Levels of GFP-RhoGDI-8, GFP-RhoGDI and endogenous RhoGDI, were assessed by Western blot. Sv, simvastatin; Chlo, chloroquine; Leu, leupeptin.CC BY · PubMed Central

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Metadata

Authors
Pérez-Sala, D., Boya, P., Ramos, I., Herrera, M., & Stamatakis, K.
Venue
PLoS ONE
Publisher
Public Library of Science (PLoS)
Published
2009-12-02
Volume
4
Issue
12
Pages
e8117
ISSN
1932-6203
DOI
10.1371/journal.pone.0008117
PMC
PMC2780327
Cited by
69
References
1
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (unspecified)

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Pérez-Sala, D., Boya, P., Ramos, I., Herrera, M., & Stamatakis, K. (2009). The C-Terminal Sequence of RhoB Directs Protein Degradation through an Endo-Lysosomal Pathway. PLoS ONE. https://doi.org/10.1371/journal.pone.0008117