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Syntaxin 1a immune complexes
1a Immune Complexes, supplied by Syntaxin, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mutant w118s
rab27a immune complexes

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Mutagenesis:

Article Title: Granuphilin Modulates the Exocytosis of Secretory Granules through Interaction with Syntaxin 1a
Article Snippet: .. In contrast, mutant W118S was barely detectable in Rab27a immune complexes but was recovered to a degree comparable to that of the wild type in syntaxin 1a immune complexes. .. On the other hand, mutant L43A was readily detected in Rab27a immunoprecipitates but was not detected in syntaxin 1a immunoprecipitates.

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  • 93
    Syntaxin autophagosomes
    Localization of STX17 is affected in the absence of LAMP-2. In LAMP-2-negative fibroblasts, STX17 could not be detected on either LC3-positive <t>autophagosomes</t> (A) or on LAMP-1-positive vesicles (B). In wild-type MEFs, STX17 is mainly present on the autophagosomes as indicated by co-localization with LC3 (C) and occasionally on LAMP-1-positive lysosomes (D). Scale bars=20 µm. Using the JACoP plugin, a significant decrease of co-localization of STX17 with LC3 was observed in the absence of LAMP-2 (E), while the overlapping of STX17 with LAMP-1 was absent in both cell types (F). Immuno-electron microscopy confirms the autophagosomal localization of STX17 (15-nm gold particle, arrowheads) in wild-type MEFs (G). Due to the low number of STX17-positive particles definitive localization could not be established in LAMP-2-single- and LAMP-1/2-double-deficient cells. Scale bars=500 nm. (G). LAMP-1 and STX17 were observed in independent vesicles in wild-type MEFs. Scale bars=200 nm (H). Data are expressed as mean±s.d. from at least 15 cells in each condition and are representative of three independent experiments. ** P
    Autophagosomes, supplied by Syntaxin, used in various techniques. Bioz Stars score: 93/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Syntaxin sec22b
    Proteins co-immunoprecipitated with <t>Sec22b</t> in a ~110 kDa complex after VTV–Golgi docking ( A ) VTVs (150 μ g) were incubated at 4 °C with hepatic cis -Golgi (300 μ g), cytosol (500 μ g of protein), and without Mg 2+ -ATP. VTV–Golgi complexes were isolated on a sucrose step gradient. VTV–Golgi complexes were solubilized in 2 % (v/v) Triton X-100 and incubated with anti-Sec22b antibodies bound to agarose beads at 4 °C overnight. The beads were washed and either not boiled (lane 1) or boiled (lane 2) in Laemmli buffer. The proteins were separated by SDS/PAGE (5–15 %) and probed with antibodies against the indicated proteins. A single membrane was used, which was sequentially probed with the indicated antibodies after washing. Only protein bands that migrated at ~ 110 kDa are shown. Detection was carried out by ECL. The results are representative of four experiments. ( B ) Samples of hepatic whole-cell lysate (WCL), VTVs, ER and Golgi (each containing 30 μ g of protein) were separated by SDS/PAGE (12 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against the indicated proteins. Protein detection was by ECL.
    Sec22b, supplied by Syntaxin, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Syntaxin snare proteins snap 23
    Knockdown of <t>SNARE</t> proteins arrests COL6 in a late-Golgi VAMP2-positive compartment. (A) Lysates from mEFs transfected with control and <t>SNAP-23</t> siRNA were analyzed by immunoblotting. β-tubulin served as a loading control (top). mEFs transfected
    Snare Proteins Snap 23, supplied by Syntaxin, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Syntaxin 1a immune complexes
    Knockdown of <t>SNARE</t> proteins arrests COL6 in a late-Golgi VAMP2-positive compartment. (A) Lysates from mEFs transfected with control and <t>SNAP-23</t> siRNA were analyzed by immunoblotting. β-tubulin served as a loading control (top). mEFs transfected
    1a Immune Complexes, supplied by Syntaxin, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Localization of STX17 is affected in the absence of LAMP-2. In LAMP-2-negative fibroblasts, STX17 could not be detected on either LC3-positive autophagosomes (A) or on LAMP-1-positive vesicles (B). In wild-type MEFs, STX17 is mainly present on the autophagosomes as indicated by co-localization with LC3 (C) and occasionally on LAMP-1-positive lysosomes (D). Scale bars=20 µm. Using the JACoP plugin, a significant decrease of co-localization of STX17 with LC3 was observed in the absence of LAMP-2 (E), while the overlapping of STX17 with LAMP-1 was absent in both cell types (F). Immuno-electron microscopy confirms the autophagosomal localization of STX17 (15-nm gold particle, arrowheads) in wild-type MEFs (G). Due to the low number of STX17-positive particles definitive localization could not be established in LAMP-2-single- and LAMP-1/2-double-deficient cells. Scale bars=500 nm. (G). LAMP-1 and STX17 were observed in independent vesicles in wild-type MEFs. Scale bars=200 nm (H). Data are expressed as mean±s.d. from at least 15 cells in each condition and are representative of three independent experiments. ** P

    Journal: Biology Open

    Article Title: LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes

    doi: 10.1242/bio.018648

    Figure Lengend Snippet: Localization of STX17 is affected in the absence of LAMP-2. In LAMP-2-negative fibroblasts, STX17 could not be detected on either LC3-positive autophagosomes (A) or on LAMP-1-positive vesicles (B). In wild-type MEFs, STX17 is mainly present on the autophagosomes as indicated by co-localization with LC3 (C) and occasionally on LAMP-1-positive lysosomes (D). Scale bars=20 µm. Using the JACoP plugin, a significant decrease of co-localization of STX17 with LC3 was observed in the absence of LAMP-2 (E), while the overlapping of STX17 with LAMP-1 was absent in both cell types (F). Immuno-electron microscopy confirms the autophagosomal localization of STX17 (15-nm gold particle, arrowheads) in wild-type MEFs (G). Due to the low number of STX17-positive particles definitive localization could not be established in LAMP-2-single- and LAMP-1/2-double-deficient cells. Scale bars=500 nm. (G). LAMP-1 and STX17 were observed in independent vesicles in wild-type MEFs. Scale bars=200 nm (H). Data are expressed as mean±s.d. from at least 15 cells in each condition and are representative of three independent experiments. ** P

    Article Snippet: The HOPS complex will then tether lysosomes to autophagosomes by cross-linking Rab7 on lysosomes to syntaxin 17 (STX17) on autophagosomes ( ) in a process augmented by Atg14 ( ; ).

    Techniques: Immuno-Electron Microscopy

    The autophagic flux is impaired in LAMP-2-single- and LAMP-1/2-double-deficient cells after autophagy induction. Cells were transfected with the tandem-fluorescent tagged mRFP–GFP–LC3 construct (A) and cultured in media (control), rapamycin (50 µm) (B) or HBSS (C) for 6 h. In wild-type MEFs, autophagy induction was characterized by an increased number of autophagosomes and autolysosomes (D) while in LAMP-2-single-deficient (E) and LAMP-1/2-double-deficient (F) cells the number of autolysosomes remained unchanged after treatment with rapamycin or HBSS. (G) Western blot analysis of total cell extract reveals an absence of degradation of p62 after rapamycin treatment confirming the blockage of the autophagic flux in LAMP-2-negative cells. Scale bars=10 µm. Data are expressed as mean±s.d. of three independent experiments. * P

    Journal: Biology Open

    Article Title: LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes

    doi: 10.1242/bio.018648

    Figure Lengend Snippet: The autophagic flux is impaired in LAMP-2-single- and LAMP-1/2-double-deficient cells after autophagy induction. Cells were transfected with the tandem-fluorescent tagged mRFP–GFP–LC3 construct (A) and cultured in media (control), rapamycin (50 µm) (B) or HBSS (C) for 6 h. In wild-type MEFs, autophagy induction was characterized by an increased number of autophagosomes and autolysosomes (D) while in LAMP-2-single-deficient (E) and LAMP-1/2-double-deficient (F) cells the number of autolysosomes remained unchanged after treatment with rapamycin or HBSS. (G) Western blot analysis of total cell extract reveals an absence of degradation of p62 after rapamycin treatment confirming the blockage of the autophagic flux in LAMP-2-negative cells. Scale bars=10 µm. Data are expressed as mean±s.d. of three independent experiments. * P

    Article Snippet: The HOPS complex will then tether lysosomes to autophagosomes by cross-linking Rab7 on lysosomes to syntaxin 17 (STX17) on autophagosomes ( ) in a process augmented by Atg14 ( ; ).

    Techniques: Transfection, Construct, Cell Culture, Western Blot

    STX17 is not found on the autophagosomes of LAMP-2 and LAMP-1/2 deficient cells. The amount of protein in the cell lysate of LAMP-2-deficient and -sufficient cells is similar (A,B), while the localization of STX17 is different. In wild-type cells, STX17 is recruited to LC3-positive autophagosome after autophagy induction (C), but it is not observed on the autophagosomes of single- and double-deficient cells (D,E). Transfection of wild-type and LAMP-2-deficient cells with the FLAG–Stx17 construct confirms the absence of STX17 recruitment into vesicles in the absence of LAMP-2 (F). This effect could be partially restored by transfection with LAMP-2A (G,H). Scale bars=20 µm. Data are expressed as mean±s.d. of three independent experiments. * P

    Journal: Biology Open

    Article Title: LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes

    doi: 10.1242/bio.018648

    Figure Lengend Snippet: STX17 is not found on the autophagosomes of LAMP-2 and LAMP-1/2 deficient cells. The amount of protein in the cell lysate of LAMP-2-deficient and -sufficient cells is similar (A,B), while the localization of STX17 is different. In wild-type cells, STX17 is recruited to LC3-positive autophagosome after autophagy induction (C), but it is not observed on the autophagosomes of single- and double-deficient cells (D,E). Transfection of wild-type and LAMP-2-deficient cells with the FLAG–Stx17 construct confirms the absence of STX17 recruitment into vesicles in the absence of LAMP-2 (F). This effect could be partially restored by transfection with LAMP-2A (G,H). Scale bars=20 µm. Data are expressed as mean±s.d. of three independent experiments. * P

    Article Snippet: The HOPS complex will then tether lysosomes to autophagosomes by cross-linking Rab7 on lysosomes to syntaxin 17 (STX17) on autophagosomes ( ) in a process augmented by Atg14 ( ; ).

    Techniques: Transfection, Construct

    Proteins co-immunoprecipitated with Sec22b in a ~110 kDa complex after VTV–Golgi docking ( A ) VTVs (150 μ g) were incubated at 4 °C with hepatic cis -Golgi (300 μ g), cytosol (500 μ g of protein), and without Mg 2+ -ATP. VTV–Golgi complexes were isolated on a sucrose step gradient. VTV–Golgi complexes were solubilized in 2 % (v/v) Triton X-100 and incubated with anti-Sec22b antibodies bound to agarose beads at 4 °C overnight. The beads were washed and either not boiled (lane 1) or boiled (lane 2) in Laemmli buffer. The proteins were separated by SDS/PAGE (5–15 %) and probed with antibodies against the indicated proteins. A single membrane was used, which was sequentially probed with the indicated antibodies after washing. Only protein bands that migrated at ~ 110 kDa are shown. Detection was carried out by ECL. The results are representative of four experiments. ( B ) Samples of hepatic whole-cell lysate (WCL), VTVs, ER and Golgi (each containing 30 μ g of protein) were separated by SDS/PAGE (12 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against the indicated proteins. Protein detection was by ECL.

    Journal: The Biochemical journal

    Article Title: The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi

    doi: 10.1042/BJ20100336

    Figure Lengend Snippet: Proteins co-immunoprecipitated with Sec22b in a ~110 kDa complex after VTV–Golgi docking ( A ) VTVs (150 μ g) were incubated at 4 °C with hepatic cis -Golgi (300 μ g), cytosol (500 μ g of protein), and without Mg 2+ -ATP. VTV–Golgi complexes were isolated on a sucrose step gradient. VTV–Golgi complexes were solubilized in 2 % (v/v) Triton X-100 and incubated with anti-Sec22b antibodies bound to agarose beads at 4 °C overnight. The beads were washed and either not boiled (lane 1) or boiled (lane 2) in Laemmli buffer. The proteins were separated by SDS/PAGE (5–15 %) and probed with antibodies against the indicated proteins. A single membrane was used, which was sequentially probed with the indicated antibodies after washing. Only protein bands that migrated at ~ 110 kDa are shown. Detection was carried out by ECL. The results are representative of four experiments. ( B ) Samples of hepatic whole-cell lysate (WCL), VTVs, ER and Golgi (each containing 30 μ g of protein) were separated by SDS/PAGE (12 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against the indicated proteins. Protein detection was by ECL.

    Article Snippet: The components of the complex were identified as Sec22b, syntaxin 5, rBet1 and GOS28.

    Techniques: Immunoprecipitation, Incubation, Isolation, SDS Page

    Incubation of VTVs with anti-Sec22b antibodies or hepatic Golgi with anti-GOS28 antibodies blocks VTV–Golgi docking and SNARE complex formation ( A ) VTVs (150 μ g of protein) containing [ 14 C]TAG were incubated at 4 °C with 10 μ l of pre-immune IgG (bar 1) or 10 μ l of anti-Sec22b antibodies (bar 2) for 1 h at 4 °C. Hepatic cis -Golgi (300 μ g of protein) was incubated at 4 °C with 10 μ l of anti-GOS28 antibodies (bar 3). In each case, the excess antibodies were removed by washing. After antibody treatment, non-radiolabelled cis -Golgi was added to tubes containing IgG-treated VTV (bar 1), Sec22b antibody-treated VTV (bar 2) and untreated [ 14 C]TAG-loaded VTVs were added to tubes containing antibody-treated cis -Golgi (bar 3). The VTV–Golgi docking reaction was carried out and the post-docking Golgi membranes were separated, and Golgi-associated [ 14 C]TAG levels were measured. Results are means + S.E.M. ( n = 4). ( B ) Post-docking Golgi membranes from ( A ) were solubilized in Laemmli buffer, and proteins were separated by SDS/PAGE and probed with anti-Sec22b antibodies. Lanes 1–3 represent the same docking conditions as applied in bars 1–3 in ( A ) respectively. ( C ) Post-docking Golgi membranes from ( A ) (bars 1 and 2) were solubilized in Laemmli buffer and proteins were separated by SDS/PAGE and probed with anti-GOS28 antibodies. Lanes 1 and 2 represents the same docking conditions as used in bars 1 and 2 in ( A ) respectively.

    Journal: The Biochemical journal

    Article Title: The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi

    doi: 10.1042/BJ20100336

    Figure Lengend Snippet: Incubation of VTVs with anti-Sec22b antibodies or hepatic Golgi with anti-GOS28 antibodies blocks VTV–Golgi docking and SNARE complex formation ( A ) VTVs (150 μ g of protein) containing [ 14 C]TAG were incubated at 4 °C with 10 μ l of pre-immune IgG (bar 1) or 10 μ l of anti-Sec22b antibodies (bar 2) for 1 h at 4 °C. Hepatic cis -Golgi (300 μ g of protein) was incubated at 4 °C with 10 μ l of anti-GOS28 antibodies (bar 3). In each case, the excess antibodies were removed by washing. After antibody treatment, non-radiolabelled cis -Golgi was added to tubes containing IgG-treated VTV (bar 1), Sec22b antibody-treated VTV (bar 2) and untreated [ 14 C]TAG-loaded VTVs were added to tubes containing antibody-treated cis -Golgi (bar 3). The VTV–Golgi docking reaction was carried out and the post-docking Golgi membranes were separated, and Golgi-associated [ 14 C]TAG levels were measured. Results are means + S.E.M. ( n = 4). ( B ) Post-docking Golgi membranes from ( A ) were solubilized in Laemmli buffer, and proteins were separated by SDS/PAGE and probed with anti-Sec22b antibodies. Lanes 1–3 represent the same docking conditions as applied in bars 1–3 in ( A ) respectively. ( C ) Post-docking Golgi membranes from ( A ) (bars 1 and 2) were solubilized in Laemmli buffer and proteins were separated by SDS/PAGE and probed with anti-GOS28 antibodies. Lanes 1 and 2 represents the same docking conditions as used in bars 1 and 2 in ( A ) respectively.

    Article Snippet: The components of the complex were identified as Sec22b, syntaxin 5, rBet1 and GOS28.

    Techniques: Incubation, SDS Page

    VTVs utilize Sec22b as a functional v-SNARE to fuse with hepatic cis -Golgi VTVs (150 μ g of protein) containing [ 14 C]TAG and [ 3 H]apoB100 were incubated at 4 °C with 10 μ l of pre-immune IgG, 10 μ l of anti-Sec22b antibodies, 10 μ l of anti-VAMP7 antibodies, 10 μ l of anti-Sar1 antibodies or 10 μ l of boiled anti-Sec22b antibodies. Antibodies in each case were removed by washing, and the treated VTVs were incubated with non-radiolabelled cis -Golgi (300 μ g of protein) at 37 °C in the presence or absence (no cyto) of cytosol (0.5 mg of protein). ( A ) After incubation, Golgi membranes were separated and the Golgi-associated [ 14 C]TAG was extracted ( A ) or the Golgi-associated [ 3 H]apoB100 was immunoprecipitated ( B ). Total [ 14 C]TAG ( A ) or [ 3 H]apoB100 ( B ) levels (in d.p.m.) were determined. For details, see the Experimental section. Results are means + S.E.M. ( n = 4).

    Journal: The Biochemical journal

    Article Title: The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi

    doi: 10.1042/BJ20100336

    Figure Lengend Snippet: VTVs utilize Sec22b as a functional v-SNARE to fuse with hepatic cis -Golgi VTVs (150 μ g of protein) containing [ 14 C]TAG and [ 3 H]apoB100 were incubated at 4 °C with 10 μ l of pre-immune IgG, 10 μ l of anti-Sec22b antibodies, 10 μ l of anti-VAMP7 antibodies, 10 μ l of anti-Sar1 antibodies or 10 μ l of boiled anti-Sec22b antibodies. Antibodies in each case were removed by washing, and the treated VTVs were incubated with non-radiolabelled cis -Golgi (300 μ g of protein) at 37 °C in the presence or absence (no cyto) of cytosol (0.5 mg of protein). ( A ) After incubation, Golgi membranes were separated and the Golgi-associated [ 14 C]TAG was extracted ( A ) or the Golgi-associated [ 3 H]apoB100 was immunoprecipitated ( B ). Total [ 14 C]TAG ( A ) or [ 3 H]apoB100 ( B ) levels (in d.p.m.) were determined. For details, see the Experimental section. Results are means + S.E.M. ( n = 4).

    Article Snippet: The components of the complex were identified as Sec22b, syntaxin 5, rBet1 and GOS28.

    Techniques: Functional Assay, Incubation, Immunoprecipitation

    Sec22b pulls down a ~110 kDa protein complex from post-docking VTV–Golgi complexes VTVs (150 μ g) were incubated at 4 °C with hepatic cis -Golgi (300 μ g), cytosol (500 μ g of protein) and without Mg 2+ -ATP. The VTV–Golgi complexes were isolated on a sucrose step gradient. The VTV–Golgi complexes were solubilized in 2 % (v/v) Triton X-100 and incubated with either pre-immune IgG or anti-Sec22b antibodies bound to agarose beads at 4 °C overnight. The beads were washed and either boiled or not, as indicated, in Laemmli buffer. The proteins were separated by SDS/PAGE (5–15 % gel) and the gel was stained. For further details, see the Experimental section. IP, immunoprecipitation.

    Journal: The Biochemical journal

    Article Title: The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi

    doi: 10.1042/BJ20100336

    Figure Lengend Snippet: Sec22b pulls down a ~110 kDa protein complex from post-docking VTV–Golgi complexes VTVs (150 μ g) were incubated at 4 °C with hepatic cis -Golgi (300 μ g), cytosol (500 μ g of protein) and without Mg 2+ -ATP. The VTV–Golgi complexes were isolated on a sucrose step gradient. The VTV–Golgi complexes were solubilized in 2 % (v/v) Triton X-100 and incubated with either pre-immune IgG or anti-Sec22b antibodies bound to agarose beads at 4 °C overnight. The beads were washed and either boiled or not, as indicated, in Laemmli buffer. The proteins were separated by SDS/PAGE (5–15 % gel) and the gel was stained. For further details, see the Experimental section. IP, immunoprecipitation.

    Article Snippet: The components of the complex were identified as Sec22b, syntaxin 5, rBet1 and GOS28.

    Techniques: Incubation, Isolation, SDS Page, Staining, Immunoprecipitation

    Sec22b concentrates on VTVs and co-localizes with p58 and Sar1 on their surface ( A ) Samples containing hepatic whole-cell lysate (WCL), VTVs, ER and Golgi (each containing30 μ g of protein) were separated by SDS/PAGE (12 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against GOS28, calnexin, and Rab11. For details, see the Experimental section. Protein detection was by ECL. ( B ) Samples of ER and VTVs (30 μ g of protein each) were separated by SDS/PAGE (5–15 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against Sec22b, Ykt6, ApoB100 and albumin. Protein detection was by ECL. ( C ) Immunoelectron microscopy of VTVs utilizing the negative-staining technique. VTVs were adsorbed on formvar-carbon-coated nickel grids and were treated with: (i) anti-rabbit pre-immune IgG; (ii) rabbit polyclonal anti-Sec22b antibodies detected with anti-(rabbit IgG) labelled with 15 nm gold particles; (iii) mouse anti-Sec22b antibodies detected with anti-(mouse IgG) labelled with 15 nm gold particles and anti-Sar1 antibodies detected with anti-(rabbit IgG) labelled with 10 nm gold particles (arrows show co-localization of Sec22b with Sar1); and (iv) anti-p58 antibodies detected with anti-(rabbit IgG) labelled with 10 nm gold particles and mouse anti-Sec22b antibodies detected with anti-(mouse IgG) labelled with 15 nm gold particles (arrows show co-localization of Sec22b with p58). Scale bars, 100 nm.

    Journal: The Biochemical journal

    Article Title: The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi

    doi: 10.1042/BJ20100336

    Figure Lengend Snippet: Sec22b concentrates on VTVs and co-localizes with p58 and Sar1 on their surface ( A ) Samples containing hepatic whole-cell lysate (WCL), VTVs, ER and Golgi (each containing30 μ g of protein) were separated by SDS/PAGE (12 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against GOS28, calnexin, and Rab11. For details, see the Experimental section. Protein detection was by ECL. ( B ) Samples of ER and VTVs (30 μ g of protein each) were separated by SDS/PAGE (5–15 % gel), transblotted on to a nitrocellulose membrane and probed with specific antibodies against Sec22b, Ykt6, ApoB100 and albumin. Protein detection was by ECL. ( C ) Immunoelectron microscopy of VTVs utilizing the negative-staining technique. VTVs were adsorbed on formvar-carbon-coated nickel grids and were treated with: (i) anti-rabbit pre-immune IgG; (ii) rabbit polyclonal anti-Sec22b antibodies detected with anti-(rabbit IgG) labelled with 15 nm gold particles; (iii) mouse anti-Sec22b antibodies detected with anti-(mouse IgG) labelled with 15 nm gold particles and anti-Sar1 antibodies detected with anti-(rabbit IgG) labelled with 10 nm gold particles (arrows show co-localization of Sec22b with Sar1); and (iv) anti-p58 antibodies detected with anti-(rabbit IgG) labelled with 10 nm gold particles and mouse anti-Sec22b antibodies detected with anti-(mouse IgG) labelled with 15 nm gold particles (arrows show co-localization of Sec22b with p58). Scale bars, 100 nm.

    Article Snippet: The components of the complex were identified as Sec22b, syntaxin 5, rBet1 and GOS28.

    Techniques: SDS Page, Immuno-Electron Microscopy, Negative Staining

    Knockdown of SNARE proteins arrests COL6 in a late-Golgi VAMP2-positive compartment. (A) Lysates from mEFs transfected with control and SNAP-23 siRNA were analyzed by immunoblotting. β-tubulin served as a loading control (top). mEFs transfected

    Journal: Journal of Cell Science

    Article Title: Annexin A2 mediates secretion of collagen VI, pulmonary elasticity and apoptosis of bronchial epithelial cells

    doi: 10.1242/jcs.137802

    Figure Lengend Snippet: Knockdown of SNARE proteins arrests COL6 in a late-Golgi VAMP2-positive compartment. (A) Lysates from mEFs transfected with control and SNAP-23 siRNA were analyzed by immunoblotting. β-tubulin served as a loading control (top). mEFs transfected

    Article Snippet: Co-immunoprecipitation and immunoelectron microscopy experiments revealed that ANXA2 and COL6 form a complex with the SNARE proteins SNAP-23, VAMP2 and syntaxin 2, which are all components of the epithelial exocytotic machinery.

    Techniques: Transfection

    ANXA2 interacts with SNAREs and enables release of COL6 from a late-Golgi VAMP2-positive compartment. (A) Anti-COL6a1,a2 immunoprecipitates from whole-lung lysates were immunoblotted with antibodies directed against COL6a1,a2, ANXA2, SNAP-23, VAMP2 and

    Journal: Journal of Cell Science

    Article Title: Annexin A2 mediates secretion of collagen VI, pulmonary elasticity and apoptosis of bronchial epithelial cells

    doi: 10.1242/jcs.137802

    Figure Lengend Snippet: ANXA2 interacts with SNAREs and enables release of COL6 from a late-Golgi VAMP2-positive compartment. (A) Anti-COL6a1,a2 immunoprecipitates from whole-lung lysates were immunoblotted with antibodies directed against COL6a1,a2, ANXA2, SNAP-23, VAMP2 and

    Article Snippet: Co-immunoprecipitation and immunoelectron microscopy experiments revealed that ANXA2 and COL6 form a complex with the SNARE proteins SNAP-23, VAMP2 and syntaxin 2, which are all components of the epithelial exocytotic machinery.

    Techniques: