XB-IMG-173147
Xenbase Image ID: 173147
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Fig. 6. March2 interacts with Dapper1 for Dsh degradation. (A) Dpr1MO impairs the March2-mediated decrease of Dsh protein. Four-cell stage embryos were dorso-animally injected with the indicated reagents and analyzed at stage 12. Amounts of injected mRNAs and MOs: GFP-XDsh, 200 pg; HA-Mar2, 1 ng; CoMO, 40 ng; Dpr1MO, 20 (+) and 40 ng (++); Dpr1, 1 (+) and 2 ng (++). (B) Mar2MO inhibits the Dpr1-mediated decrease in Dsh. Amounts of injected mRNAs and MOs: GFP-XDsh, 200 pg; Mar2, 1 ng; CoMO and Mar2MO, 40 ng; Dpr1, 2 ng. (C) The dominant-negative (DN) form of Dpr1 inhibits the March2-mediated decrease of Dsh. Amounts of injected mRNAs: GFP-Dsh, 200 pg; Mar2, 1 ng; DN Dpr1, 2 ng. (D) In vivo ubiquitylation assays showing that Dpr1MO (40 ng) reduces Mar2-mediated poly-ubiquitylation of Dsh. (E) Co-immunoprecipitation analysis showing that March2 binds Dpr1 in HEK293 T cells. (F-J) Dsh, Dpr1 and March2 are colocalized in Xenopus. Animal caps injected with GFP-XDsh (250 pg), Myc-Dpr1 (250 pg) and HA-Mar2 (250 pg) mRNAs were analyzed. White arrows (J) indicate Dsh-Dpr1-Mar2 colocalized puncta. (K) Co-immunoprecipitation analysis in Xenopus embryos showing Dpr1MO weakens the binding affinity between Mar2 and Dsh. Amounts of injected mRNAs and MOs: GFP-XDsh, 1 ng; HA-Mar2,1 ng; CoMO and Dpr1MO, 40 ng. Image published in: Lee H et al. (2018) Copyright © 2018. Image reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View |