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ultrastructural localization  (Addgene inc)

 
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    Addgene inc ultrastructural localization
    ( A ) Lentiviral expression of a truncated STAR lacking its mitochondrial targeting sequence ( ΔN62- STAR) fused to the outer mitochondrial membrane (OMM) anchor TOM20 fails to rescue Bt 2 cAMP-induced steroidogenesis in STAR-deficient MA-10 STKO cells, in contrast to reconstitution with native STAR (positive control, pC; negative control, nC; different alphabets indicate significant difference p<0.05). Immunoblot confirms expression of the TOM20 -ΔN62- STAR fusion protein at the expected molecular weight (∼41.2 kDa). This contrasts with previous claims that this construct yields maximal constitutive steroid production. (B) Sequence comparisons between the STAR MTS and the well-characterized bipartite MTS of cytochrome C1 (CYTC1 MTS ) reveal conserved features, including a mitochondrial processing peptidase (MPP) cleavage site and a predicted inner membrane peptidase (IMP) site. These conserved elements support a stop-transfer import mechanism characteristic of proteins targeted to the mitochondrial intermembrane space (IMS). The accompanying schematic illustrates the principle of this stop-transfer mechanism, where translocases at the outer and inner mitochondrial membranes mediate import ①, and MPP-mediated cleavage ②, the sorting signal anchors to the IMM ③, followed by IMP-mediated cleavage ④, and IMS release ⑤. (C) Confocal imaging demonstrates mitochondrial colocalization of CYTC1 MTS-ΔN62- STAR-Emerald with the OMM marker TOM20-mRuby in MA-10 cells, confirming successful targeting to mitochondria using the CYTC1 MTS . (D) Functional rescue of steroidogenesis is achieved in MA-10 STKO cells by CYTC1 MTS-ΔN62- STAR, showing equivalence to native STAR in restoring progesterone production, thereby demonstrating that IMS localization fully restores STAR function (different alphabets indicate significant difference p<0.05). Western blot analysis shows identical of mitochondrial processing of native STAR and CYTC1 MTS-ΔN62- STAR. (E) APEX2-based <t>ultrastructural</t> labeling distinguishes STAR sub-mitochondrial localization: TOM20-APEX2 marks the cytoplasmic face of the OMM; N36- STAR-APEX2, containing only the presequence, targets the matrix; native STAR-APEX2 localizes specifically to the IMS. This confirms that the full STAR MTS directs import via a stop-transfer mechanism, releasing STAR into the IMS for its functional role.
    Ultrastructural Localization, supplied by Addgene inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "STAR/STARD1: a mitochondrial intermembrane space cholesterol shuttle degraded through mitophagy"

    Article Title: STAR/STARD1: a mitochondrial intermembrane space cholesterol shuttle degraded through mitophagy

    Journal: bioRxiv

    doi: 10.1101/2025.04.03.647084

    ( A ) Lentiviral expression of a truncated STAR lacking its mitochondrial targeting sequence ( ΔN62- STAR) fused to the outer mitochondrial membrane (OMM) anchor TOM20 fails to rescue Bt 2 cAMP-induced steroidogenesis in STAR-deficient MA-10 STKO cells, in contrast to reconstitution with native STAR (positive control, pC; negative control, nC; different alphabets indicate significant difference p<0.05). Immunoblot confirms expression of the TOM20 -ΔN62- STAR fusion protein at the expected molecular weight (∼41.2 kDa). This contrasts with previous claims that this construct yields maximal constitutive steroid production. (B) Sequence comparisons between the STAR MTS and the well-characterized bipartite MTS of cytochrome C1 (CYTC1 MTS ) reveal conserved features, including a mitochondrial processing peptidase (MPP) cleavage site and a predicted inner membrane peptidase (IMP) site. These conserved elements support a stop-transfer import mechanism characteristic of proteins targeted to the mitochondrial intermembrane space (IMS). The accompanying schematic illustrates the principle of this stop-transfer mechanism, where translocases at the outer and inner mitochondrial membranes mediate import ①, and MPP-mediated cleavage ②, the sorting signal anchors to the IMM ③, followed by IMP-mediated cleavage ④, and IMS release ⑤. (C) Confocal imaging demonstrates mitochondrial colocalization of CYTC1 MTS-ΔN62- STAR-Emerald with the OMM marker TOM20-mRuby in MA-10 cells, confirming successful targeting to mitochondria using the CYTC1 MTS . (D) Functional rescue of steroidogenesis is achieved in MA-10 STKO cells by CYTC1 MTS-ΔN62- STAR, showing equivalence to native STAR in restoring progesterone production, thereby demonstrating that IMS localization fully restores STAR function (different alphabets indicate significant difference p<0.05). Western blot analysis shows identical of mitochondrial processing of native STAR and CYTC1 MTS-ΔN62- STAR. (E) APEX2-based ultrastructural labeling distinguishes STAR sub-mitochondrial localization: TOM20-APEX2 marks the cytoplasmic face of the OMM; N36- STAR-APEX2, containing only the presequence, targets the matrix; native STAR-APEX2 localizes specifically to the IMS. This confirms that the full STAR MTS directs import via a stop-transfer mechanism, releasing STAR into the IMS for its functional role.
    Figure Legend Snippet: ( A ) Lentiviral expression of a truncated STAR lacking its mitochondrial targeting sequence ( ΔN62- STAR) fused to the outer mitochondrial membrane (OMM) anchor TOM20 fails to rescue Bt 2 cAMP-induced steroidogenesis in STAR-deficient MA-10 STKO cells, in contrast to reconstitution with native STAR (positive control, pC; negative control, nC; different alphabets indicate significant difference p<0.05). Immunoblot confirms expression of the TOM20 -ΔN62- STAR fusion protein at the expected molecular weight (∼41.2 kDa). This contrasts with previous claims that this construct yields maximal constitutive steroid production. (B) Sequence comparisons between the STAR MTS and the well-characterized bipartite MTS of cytochrome C1 (CYTC1 MTS ) reveal conserved features, including a mitochondrial processing peptidase (MPP) cleavage site and a predicted inner membrane peptidase (IMP) site. These conserved elements support a stop-transfer import mechanism characteristic of proteins targeted to the mitochondrial intermembrane space (IMS). The accompanying schematic illustrates the principle of this stop-transfer mechanism, where translocases at the outer and inner mitochondrial membranes mediate import ①, and MPP-mediated cleavage ②, the sorting signal anchors to the IMM ③, followed by IMP-mediated cleavage ④, and IMS release ⑤. (C) Confocal imaging demonstrates mitochondrial colocalization of CYTC1 MTS-ΔN62- STAR-Emerald with the OMM marker TOM20-mRuby in MA-10 cells, confirming successful targeting to mitochondria using the CYTC1 MTS . (D) Functional rescue of steroidogenesis is achieved in MA-10 STKO cells by CYTC1 MTS-ΔN62- STAR, showing equivalence to native STAR in restoring progesterone production, thereby demonstrating that IMS localization fully restores STAR function (different alphabets indicate significant difference p<0.05). Western blot analysis shows identical of mitochondrial processing of native STAR and CYTC1 MTS-ΔN62- STAR. (E) APEX2-based ultrastructural labeling distinguishes STAR sub-mitochondrial localization: TOM20-APEX2 marks the cytoplasmic face of the OMM; N36- STAR-APEX2, containing only the presequence, targets the matrix; native STAR-APEX2 localizes specifically to the IMS. This confirms that the full STAR MTS directs import via a stop-transfer mechanism, releasing STAR into the IMS for its functional role.

    Techniques Used: Expressing, Sequencing, Membrane, Positive Control, Negative Control, Western Blot, Molecular Weight, Construct, Imaging, Marker, Functional Assay, Labeling



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    ( A ) Lentiviral expression of a truncated STAR lacking its mitochondrial targeting sequence ( ΔN62- STAR) fused to the outer mitochondrial membrane (OMM) anchor TOM20 fails to rescue Bt 2 cAMP-induced steroidogenesis in STAR-deficient MA-10 STKO cells, in contrast to reconstitution with native STAR (positive control, pC; negative control, nC; different alphabets indicate significant difference p<0.05). Immunoblot confirms expression of the TOM20 -ΔN62- STAR fusion protein at the expected molecular weight (∼41.2 kDa). This contrasts with previous claims that this construct yields maximal constitutive steroid production. (B) Sequence comparisons between the STAR MTS and the well-characterized bipartite MTS of cytochrome C1 (CYTC1 MTS ) reveal conserved features, including a mitochondrial processing peptidase (MPP) cleavage site and a predicted inner membrane peptidase (IMP) site. These conserved elements support a stop-transfer import mechanism characteristic of proteins targeted to the mitochondrial intermembrane space (IMS). The accompanying schematic illustrates the principle of this stop-transfer mechanism, where translocases at the outer and inner mitochondrial membranes mediate import ①, and MPP-mediated cleavage ②, the sorting signal anchors to the IMM ③, followed by IMP-mediated cleavage ④, and IMS release ⑤. (C) Confocal imaging demonstrates mitochondrial colocalization of CYTC1 MTS-ΔN62- STAR-Emerald with the OMM marker TOM20-mRuby in MA-10 cells, confirming successful targeting to mitochondria using the CYTC1 MTS . (D) Functional rescue of steroidogenesis is achieved in MA-10 STKO cells by CYTC1 MTS-ΔN62- STAR, showing equivalence to native STAR in restoring progesterone production, thereby demonstrating that IMS localization fully restores STAR function (different alphabets indicate significant difference p<0.05). Western blot analysis shows identical of mitochondrial processing of native STAR and CYTC1 MTS-ΔN62- STAR. (E) APEX2-based ultrastructural labeling distinguishes STAR sub-mitochondrial localization: TOM20-APEX2 marks the cytoplasmic face of the OMM; N36- STAR-APEX2, containing only the presequence, targets the matrix; native STAR-APEX2 localizes specifically to the IMS. This confirms that the full STAR MTS directs import via a stop-transfer mechanism, releasing STAR into the IMS for its functional role.

    Journal: bioRxiv

    Article Title: STAR/STARD1: a mitochondrial intermembrane space cholesterol shuttle degraded through mitophagy

    doi: 10.1101/2025.04.03.647084

    Figure Lengend Snippet: ( A ) Lentiviral expression of a truncated STAR lacking its mitochondrial targeting sequence ( ΔN62- STAR) fused to the outer mitochondrial membrane (OMM) anchor TOM20 fails to rescue Bt 2 cAMP-induced steroidogenesis in STAR-deficient MA-10 STKO cells, in contrast to reconstitution with native STAR (positive control, pC; negative control, nC; different alphabets indicate significant difference p<0.05). Immunoblot confirms expression of the TOM20 -ΔN62- STAR fusion protein at the expected molecular weight (∼41.2 kDa). This contrasts with previous claims that this construct yields maximal constitutive steroid production. (B) Sequence comparisons between the STAR MTS and the well-characterized bipartite MTS of cytochrome C1 (CYTC1 MTS ) reveal conserved features, including a mitochondrial processing peptidase (MPP) cleavage site and a predicted inner membrane peptidase (IMP) site. These conserved elements support a stop-transfer import mechanism characteristic of proteins targeted to the mitochondrial intermembrane space (IMS). The accompanying schematic illustrates the principle of this stop-transfer mechanism, where translocases at the outer and inner mitochondrial membranes mediate import ①, and MPP-mediated cleavage ②, the sorting signal anchors to the IMM ③, followed by IMP-mediated cleavage ④, and IMS release ⑤. (C) Confocal imaging demonstrates mitochondrial colocalization of CYTC1 MTS-ΔN62- STAR-Emerald with the OMM marker TOM20-mRuby in MA-10 cells, confirming successful targeting to mitochondria using the CYTC1 MTS . (D) Functional rescue of steroidogenesis is achieved in MA-10 STKO cells by CYTC1 MTS-ΔN62- STAR, showing equivalence to native STAR in restoring progesterone production, thereby demonstrating that IMS localization fully restores STAR function (different alphabets indicate significant difference p<0.05). Western blot analysis shows identical of mitochondrial processing of native STAR and CYTC1 MTS-ΔN62- STAR. (E) APEX2-based ultrastructural labeling distinguishes STAR sub-mitochondrial localization: TOM20-APEX2 marks the cytoplasmic face of the OMM; N36- STAR-APEX2, containing only the presequence, targets the matrix; native STAR-APEX2 localizes specifically to the IMS. This confirms that the full STAR MTS directs import via a stop-transfer mechanism, releasing STAR into the IMS for its functional role.

    Article Snippet: Fusions of STAR with an engineered ascorbate peroxidase (APEX2) for ultrastructural localization was cloned from mito-V5-APEX2 (72480; Addgene) downstream of native and N36-STAR in the pMX retroviral vector (pMX-STAR-APEX2, pMX-N36-APEX2).

    Techniques: Expressing, Sequencing, Membrane, Positive Control, Negative Control, Western Blot, Molecular Weight, Construct, Imaging, Marker, Functional Assay, Labeling