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Itch E3 Ubiquitin Ligase Regulates Large Tumor Suppressor 1 Tumor-Suppressor Stability

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Itch E3 Ubiquitin Ligase Regulates Large Tumor Suppressor 1 Tumor-Suppressor Stability Corrections CELL BIOLOGY Correction for “Itch E3 ubiquitin ligase regulates large tumor There were also some textual errors. On page 4870, right suppressor 1 tumor-suppressor stability,” by King Ching Ho, column, first full paragraph of the Results section, line 20 “(Fig. Zhonghua Zhou, Yi-Min She, Alex Chun, Terry D. Cyr, and 1A)” should instead appear as “(Fig. 1, A and B).” On page 4871, Xiaolong Yang, which appeared in issue 12, March 22, 2011 of left column, first partial paragraph, line 1 “(Fig. 1A)” should Proc Natl Acad Sci USA (108:4870–4875; first published March 7, instead appear as “(Fig. 1C).” On page 4871, left column, first 2011; 10.1073/pnas.1101273108). partial paragraph, line 10 “(Fig. 1B)” should instead appear as The authors note that the title appeared incorrectly. The title “(Fig. 1D).” should instead appear as “Itch E3 ubiquitin ligase regulates large Additionally, the legends for Figures 2 and 5 appeared tumor suppressor 1 stability.” The title in the online version has incorrectly. The figures and their corrected legends been corrected. appear below. Fig. 5. Itch promotes polyubiquitination and subsequent degradation of LATS1 by 26S proteasome. (A) In vitro ubiquitination of LATS1 by Itch. Im- A Fig. 2. Interaction of LATS1 and Itch in vivo and in vitro. ( ) Interaction of munoprecipitated LATS1-myc on beads was used as a substrate in an ubiq- ectopically expressed LATS1 and Itch. COS7 lysates expressing either LATS1- uitination assay with a ligase buffer containing E1, E2, Ubiquitin-FLAG, ATP, FLAG alone or together with Itch-Myc or Itch-C830A-Myc were im- and Itch-GST or Itch-C830A-GST. After reaction, the beads containing LATS1- munoprecipitated with anti-Myc antibody, followed by Western blotting myc were washed extensively with modified RIPA buffer, followed by with anti-FLAG antibody. Ponceau S staining of antibody heavy chain in- Western blot analysis using anti-FLAG antibody. (B) In vivo ubiquitination of B dicates equal amounts of anti-Myc antibody were used. ( ) Interaction of LATS1 by Itch. Ubiquitin-HA and different combinations of Itch-Myc, Itch- endogenous LATS1 and Itch. Protein lysates from MDA-MB-231 cells were ligase-dead mutant (Itch-C830A-Myc), and LATS1-FLAG were transfected immunoprecipitated with either control anti-FLAG antibody or anti-LATS1 into COS7 cells. Ubiquitinated LATS1 was detected by immunoprecipitation C antibody, followed by Western blotting with anti-Itch antibody. ( )Im- of LATS1 with anti-FLAG antibody, followed by detection of ubiquitin using munostaining analysis of LATS1 and Itch. LATS1-FLAG and Itch-Myc were anti-HA antibody. (C) Proteasome inhibitor blocks Itch-induced LATS1 deg- cotransfected into COS7 cells, followed by immunostaining with anti-FLAG radation. COS7 cells transfected with either LATS1-FLAG alone or LATS1- and anti-Myc primary antibodies and AF488 anti-mouse IgG and AF555 anti- FLAG together with Itch-Myc were treated with either DMSO (control) or D rabbit IgG secondary antibodies. ( ) GST-pulldown analysis of interaction of proteasome inhbitor (MG132). (D) Lysosome inhibitor fails to block Itch- LATS1 and Itch in vitro. COS7 lysates expressing wild-type (LATS1-WT-FLAG), induced LATS1 degradation. COS7 cells transfected with either LATS1-FLAG single-PPxY mutants (LATS1-Y376F-FLAG or LATS1-Y559F-FLAG), or double alone or LATS1-FLAG together with Itch-Myc were treated with either DMSO PPxY mutant (LATS1-Y376F-Y559F-FLAG) of LATS1 were pulled down with (control) or lysosome inhibitor (Baf A1). GST, GST-Itch, GST-Itch-WW-mutant, or GST-WW, followed by Western blotting for LATS1-FLAG using anti-FLAG antibody. 1/10 input (10 μg) rep- www.pnas.org/cgi/doi/10.1073/pnas.1105373108 resents 1/10 of protein lysate (100 μg) used for GST pulldown. 8914–8915 | PNAS | May 24, 2011 | vol. 108 | no. 21 www.pnas.org Downloaded by guest on October 1, 2021 PLANT BIOLOGY Correction for “Plant intracellular innate immune receptor Re- A B sistance to Pseudomonas syringae pv. maculicola 1 (RPM1) is acti- vated at, and functions on, the plasma membrane,” by Zhiyoug Gao, myristoylation palmitoylation Eui-Hwan Chung, Timothy K. Eitas, and Jeffery L. Dangl, which ap- peared in issue 18, May 3, 2011, of Proc Natl Acad Sci USA (108:7619– CBL tag MGCFHSKAAKEF mCBL tag MASFHSKAAKEF T S M T S M T S M 7624; first published April 13, 2011; 10.1073/pnas.1104410108). IB: α-myc The authors note there were some errors within the main IB: α-COXII manuscript text. On page 7622, right column, second full para- Rubisco graph, line 2, “35S promoter” should instead appear as “35S promoter”; on page 7622, right column, second full paragraph, CD line 7, “CBL-RPM” should instead appear as “CBL-RPM1”; and on page 7624, left column, fourth full paragraph, line 7 “anti- histone 3H” should instead appear as “anti-histone H3.” T S M T S M T S M The authors also note that the author name Zhiyoug Gao PM EM PM EM PM EM PM EM IB: α-myc should have appeared as Zhiyong Gao. The corrected author line IB: α-myc IB: α-COXII IB: α-ATPase appears below. Rubisco IB: α-COXII Additionally, the legends for Figure 4 and Figure 5 appeared IB: α-BIP incorrectly. The figures and their corrected legends appear below. Both the print article and the online version have been cor- E F 180 CBL-R1(G205E/D505V)+R4+AvrRpm1 rected to reflect these changes. These errors do not affect the mCBL-R1+R4+AvrRpm1 160 CBL-R1+R4+AvrRpm1 conclusions of the article. 140 R1+R4+AvrRpm1 120 Zhiyong Gao, Eui-Hwan Chung, Timothy K. Eitas, and 100 Jeffery L. Dangl 80 IB: α-myc 60 Rubisco 40 IB: α-RIN4 Conductivity (μS/cm) Conductivity 20 IB: α-HA 0 4 8 12 16 20 T7-R1(D505V)-YFP 35S:PLC2-CFP Merge Bright Field Time post induction (hours) + AvrRpm1-HA / RIN4 Fig. 5. Plasma membrane-tethered RPM1 retains effector-mediated HR 4hpi function in N. benthamiana.(A). CBL tag contains dual lipid modification sites. B ( ) The CBL tag tethers soluble RPM1(G205E/D505V)-Myc to the microsomal CORRECTIONS membrane following conditional transient expression in N. benthamiama. (C) CBL and mCBL tags do not affect the membrane localization of RPM1-Myc. (D) CBL-tagged proteins localize on the plasma membrane. For B–D, proteins 4.5hpi were transiently expressed in N. benthamiana under the control of 35S pro- moter (OD600 = 0.5). Samples were collected at 40 h after agrobacteria infiltration. (E) The HR function of CBL-tagged RPM1. CBL- or mCBL-tagged RPM1-myc (R1) under the control of 35S promoter, T7-RIN4 (R4) under the control of its native promoter, and AvrRpm1-HA (AvrRpm1) under the control 5hpi of a Dex inducible promoter were co-expressed in N. benthamiana (OD600 = 0.5, 0.3, and 0.05, respectively). AvrRpm1 was induced with 20 μM Dex at 36 h after infiltration. (F) The expression level of the constructs. The protein levels of the tagged RPM1 and RIN4 were detected at 2 h after induction. The protein T7-RPM1-YFP 35S:PLC2-CFP Merge Bright Field levels of AvrRpm1 were detected at 6 h after induction. www.pnas.org/cgi/doi/10.1073/pnas.1106668108 6hpi Fig. 4. T7-RPM1(D505V)-YFP localizes to the plasma membrane of N. ben- thamiana epidermal cells. Transient expression of T7-RPM1(D505V)-YFP or T7-RPM1-YFP (OD600 = 0.3) was induced with 20 μM estradiol at 48 h after agrobacteria infiltration. Images were collected at the time after induction noted at left. 35S:PLC2-CFP (OD600 = 0.3) was co-expressed as a plasma membrane marker. PNAS | May 24, 2011 | vol. 108 | no. 21 | 8915 Downloaded by guest on October 1, 2021 Correction CELL BIOLOGY Correction for “Itch E3 ubiquitin ligase regulates large tumor sup- The authors wish to note: “There is an error on the fourth panel pressor 1 stability,” by King Ching Ho, Zhonghua Zhou, Yi-Min of Fig. 2, the Ponceau S staining figure. We have now replaced it She, Alex Chun, Terry D. Cyr, and Xiaolong Yang, which appeared with a correct figure.” As a result, Fig. 2 has been corrected. The in issue 12, March 22, 2011, of Proc Natl Acad Sci USA (108:4870– corrected figure and its legend appear below. 4875; first published March 7, 2011; 10.1073/pnas.1101273108). Fig. 2. Interaction of LATS1 and Itch in vivo and in vitro. (A) Interaction of ectopically expressed LATS1 and Itch. COS7 lysates expressing either LATS1-FLAG alone or together with Itch-Myc or Itch-C830A-Myc were immunoprecipitated with anti-Myc antibody, followed by Western blotting with anti-FLAG antibody. Ponceau S staining of antibody heavy chain indicates equal amounts of anti-Myc antibody were used. (B) Interaction of endogenous LATS1 and Itch. Protein lysates from MDA-MB-231 cells were immunoprecipitated with either control anti-FLAG antibody or anti-LATS1 antibody, followed by Western blotting with anti-Itch antibody. (C) Immunostaining analysis of LATS1 and Itch. LATS1-FLAG and Itch-Myc were cotransfected into COS7 cells, followed by immunostaining with anti-FLAG and anti-Myc primary antibodies and AF488 anti-mouse IgG and AF555 anti-rabbit IgG secondary antibodies. (D) GST-pulldown analysis of interaction of LATS1 and Itch in vitro. COS7 lysates expressing wild-type (LATS1-WT-FLAG), single-PPxY mutants (LATS1-Y376F-FLAG or LATS1-Y559F-FLAG), or double PPxY mutant (LATS1-Y376F-Y559F-FLAG) of LATS1 were pulled down with GST, GST-Itch, GST-Itch-WW-mutant, or GST-WW, followed by Western blotting for LATS1-FLAG using anti-FLAG antibody. 1/10 input (10 μg) represents 1/10 of protein lysate (100 μg) used for GST pulldown.
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