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. 2013 Nov;33(21):4308–4320. doi: 10.1128/MCB.00628-13

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Copyright © 2013, American Society for Microbiology. All Rights Reserved.

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Fig 1 — SORLA interacts with the furin-binding region in PACS1. (A) PACS1 constructs used for binding domain mapping. ARR, atrophin-1-related region; FBR, furin-binding region; MR, middle region; CTR, carboxyl-terminal region. (B) CHO cells stably expressing human SORLA were transiently transfected with constructs encoding hemagglutinin (HA)-tagged versions of ARR (ARR-HA; lane 1), FBR (FBR-HA; lane 2), and MR (MR-HA; lane 3) of PACS1. Cells transfected with the empty vector (lane 4) or with a vector encoding full-length, HA-tagged PACS1 (PACS1-HA; lane 5) were used as negative and positive controls, respectively. The input part of the panel represents Western blot analyses for SORLA (α-SORLA) and PACS1 variants (α-HA) in cell extracts prior to immunoprecipitation. The IP-SORLA part of the panel shows Western blot analyses for SORLA (α-SORLA) and PACS1 variants (α-HA) in samples immunoprecipitated with anti-SORLA IgG. Full-length PACS1 (lane 5) and the FBR domain (lane 2) are coprecipitated with SORLA. No coimmunoprecipitation is seen for ARR (lane 1) or MR (lane 3) or for the FBR when the anti-SORLA IgG was omitted (lane 6). The migration of marker proteins of the indicated molecular masses is shown. w/o, without. (C) CHO cells expressing human SORLA were transiently transfected with constructs encoding wild-type PACS1 (PACS1-HA, lane 1) or a deletion mutant form lacking the FBR (ΔFBR-HA, lane 2). The input part of the panel represents Western blot analyses for SORLA (α-SORLA) and PACS1 variants (α-HA) in cell extracts prior to immunoprecipitation. The IP-SORLA part of the panel shows Western blot analyses for SORLA (α-SORLA) and PACS1 variants (α-HA) in samples immunoprecipitated with anti-SORLA IgG. Efficient coimmunoprecipitation for full-length PACS1-HA (lane 1) but very little for ΔFBR-HA (lane 2) was seen. (D) Endogenous PACS1 and SORLA coimmunoprecipitate from brain lysate. The IP-PACS1 part of the panel shows that immunoprecipitation of PACS1 (α-PACS1) coprecipitates SORLA (α-SORLA) from wild-type (Sorl1^+/+; lane 1) but not from SORLA-deficient (Sorl1^−/−; lane 2) mouse brains. Also, no coimmunoprecipitation of SORLA from Sorl1^+/+ brains was seen in the absence of anti-PACS1 antiserum (lane 3). The input part of the panel represents Western blot analyses for SORLA and PACS1 in tissue samples prior to immunoprecipitation.