ATP5PO encodes the oligomycin sensitivity conferral protein (OSCP), also called ATP synthase subunit O, the subunit at the top of the peripheral (stator) stalk of the mitochondrial F1Fo ATP synthase (Complex V). Synthesized with an N-terminal mitochondrial targeting sequence and imported to the mitochondrial inner membrane, OSCP caps the soluble F1 catalytic head and, together with the b, d and F6 subunits, forms the stationary peripheral stalk that holds the F1 alpha3beta3 catalytic hexamer static against the rotating central stalk. This stator function is essential for coupling proton flow through the membrane Fo domain to ATP synthesis in F1 and confers the complex's sensitivity to the inhibitor oligomycin. OSCP is a structural, non-catalytic subunit; its ATP hydrolase activity is only observed as an artificial in vitro reverse reaction of the whole complex. Loss-of-function variants cause mitochondrial complex V deficiency, and OSCP is implicated in permeability transition pore regulation through its interaction with cyclophilin D.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005198 structural molecule activity | IDA PMID:7490082 Cloning of the cDNA for the human ATP synthase OSCP subunit ... | NEW | Summary: OSCP is a non-catalytic structural subunit of the ATP synthase peripheral (stator) stalk; its molecular function is structural molecule activity, contributing to the structural integrity of Complex V. This term is not currently in GOA and is proposed here as the correct subunit-level molecular function for OSCP. Reason: The existing GOA molecular-function annotations for OSCP are either the catalytic rotational ATP synthase activity (which OSCP contributes_to but does not enable) or uninformative protein binding. OSCP's own molecular function is structural: it holds the F1 catalytic head static against the rotor. Structural molecule activity (GO:0005198) captures this correctly and is used as the core molecular function. Supporting Evidence: PMID:7490082 This ATP5O subunit is a key structural component of the stalk of the mitochondrial respiratory chain file:human/ATP5PO/ATP5PO-uniprot.txt a stationary peripheral stalk (subunits F6, b, d, and |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetically inferred mitochondrial localization. OSCP is a subunit of the inner-membrane ATP synthase, so mitochondrial localization is correct, though the more specific mitochondrial inner membrane term is preferable. Reason: OSCP is an established subunit of the mitochondrial F1Fo ATP synthase, confirmed by immunocapture and cryo-EM structure of the complex. Mitochondrion is correct but general; the inner-membrane annotations capture the precise location. Supporting Evidence: PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of PMID:37244256 Biological energy currency ATP is produced by F1Fo-ATP synthase |
| GO:0046933 proton-transporting ATP synthase activity, rotational mechanism | IBA GO_REF:0000033 | ACCEPT | Summary: OSCP contributes to the rotational ATP synthase molecular function as a structural (stator) subunit of the catalytic complex, without itself being catalytic. The contributes_to qualifier is the correct usage for a non-catalytic subunit of a complex that carries the activity. Reason: OSCP is part of the peripheral stalk that holds the catalytic F1 head static against the rotor, so it contributes to (does not enable) the rotary ATP synthase activity. The contributes_to qualifier appropriately reflects that OSCP is a required structural component of the complex bearing this activity rather than the catalytic subunit itself. Supporting Evidence: file:human/ATP5PO/ATP5PO-uniprot.txt a stationary peripheral stalk (subunits F6, b, d, and PMID:12110673 The captured complex V displayed ATP hydrolysis activity that was |
| GO:0042776 proton motive force-driven mitochondrial ATP synthesis | IBA GO_REF:0000033 | ACCEPT | Summary: OSCP is involved in proton motive force-driven mitochondrial ATP synthesis as an essential structural subunit of Complex V. This is the core biological process for the gene. Reason: As the stator-stalk subunit coupling proton flow to F1 catalysis, OSCP is required for mitochondrial ATP synthesis. Knockdown/loss functionally impairs the complex, and OSCP is the target through which the F1Fo-ATPase inhibitor Bz-423 acts. Supporting Evidence: PMID:15850986 reconstitution experiments demonstrated that inhibition was mediated by the file:human/ATP5PO/ATP5PO-uniprot.txt complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt SubCell mapping of mitochondrial localization. Correct but general. Reason: Consistent with all experimental localization evidence placing OSCP in the mitochondrion (inner membrane); the general mitochondrion term is acceptable. Supporting Evidence: file:human/ATP5PO/ATP5PO-uniprot.txt Subunit OSCP, of the mitochondrial membrane ATP synthase |
| GO:0005743 mitochondrial inner membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt SubCell mapping to the mitochondrial inner membrane, the anatomical location of the ATP synthase complex. This is the precise, correct location for OSCP. Reason: The F1Fo ATP synthase is embedded in the mitochondrial inner membrane, with OSCP capping the F1 head on the matrix side of the peripheral stalk. Corroborated by Reactome TAS and ComplexPortal annotations. Supporting Evidence: PMID:26297831 the stator casings fixed with the peripheral stator stalk |
| GO:0015986 proton motive force-driven ATP synthesis | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO mapping to proton motive force-driven ATP synthesis, the parent of the mitochondrion-specific term. Correct for OSCP as an ATP synthase subunit. Reason: Broadly correct; the more specific GO:0042776 (mitochondrial) is also annotated and is the preferred core term, but this general parent is not wrong. Supporting Evidence: file:human/ATP5PO/ATP5PO-uniprot.txt complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP |
| GO:0016020 membrane | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: InterPro2GO generic membrane localization. Not wrong but uninformative given the specific mitochondrial inner membrane annotations. Reason: The generic 'membrane' term adds no information beyond the specific mitochondrial inner membrane annotations already present and should be treated as an over-annotation. Supporting Evidence: file:human/ATP5PO/ATP5PO-uniprot.txt a stationary peripheral stalk (subunits F6, b, d, and |
| GO:0046933 proton-transporting ATP synthase activity, rotational mechanism | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: InterPro2GO annotation asserting OSCP enables the rotational ATP synthase activity. OSCP is a non-catalytic structural subunit and does not itself enable this catalytic molecular function; the contributes_to formulation (also annotated) is the correct one, so the 'enables' assertion over-annotates the subunit. Reason: OSCP does not catalyze ATP synthesis; it is a stator-stalk structural subunit. The 'enables' qualifier for the rotary catalytic MF over-assigns catalytic activity to a structural subunit. The activity is better represented by the contributes_to annotations to the same term, and OSCP's own molecular function is structural molecule activity (captured in core_functions). Supporting Evidence: PMID:7490082 This ATP5O subunit is a key structural component of the stalk of the mitochondrial respiratory chain |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | MARK AS OVER ANNOTATED | Summary: Bare 'protein binding' from a high-throughput interactome dataset (interactor PNMA1). Uninformative molecular function term. Reason: Per curation guidelines, bare protein binding tells us nothing about OSCP's actual function. The interaction is from a large-scale screen with no specific functional interpretation; not removed per policy, but flagged as uninformative. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MARK AS OVER ANNOTATED | Summary: Bare 'protein binding' from a proteome-scale binary interactome map (multiple interactors). Uninformative molecular function term. Reason: Large-scale interactome mapping yields a generic protein-binding annotation without functional specificity; retained per policy but flagged as uninformative. |
| GO:0005515 protein binding | IPI PMID:27499296 Mitochondrial Protein Interaction Mapping Identifies Regulat... | MARK AS OVER ANNOTATED | Summary: Bare 'protein binding' from a mitochondrial protein interaction map (interactor ATP5F1A/subunit alpha). The alpha-subunit interaction is biologically meaningful (OSCP caps the F1 alpha3beta3 head), but the annotation term itself is uninformative. Reason: The interaction with the F1 alpha subunit is consistent with OSCP's structural role, but 'protein binding' conveys no functional information. Retained per policy, flagged as uninformative; the structural role is captured by the core annotations. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | MARK AS OVER ANNOTATED | Summary: Bare 'protein binding' from crosslinking mass spectrometry (interactor ATP5F1A). Uninformative molecular function term. Reason: Generic protein-binding annotation without functional specificity; retained per policy but flagged as uninformative. |
| GO:0005515 protein binding | IPI PMID:30266287 Cyclophilin D deficiency attenuates mitochondrial F1Fo ATP s... | MARK AS OVER ANNOTATED | Summary: 'Protein binding' capturing the OSCP interaction with cyclophilin D (PPID) and with amyloid-beta (APP). This interaction is functionally meaningful, linking OSCP to permeability transition pore regulation and to F1Fo ATP synthase dysfunction in Alzheimer's disease, but the bare GO term is uninformative. Reason: The cyclophilin D / amyloid-beta interactions are biologically important but the annotation term 'protein binding' does not convey this. Retained per policy and flagged; the functional significance is documented rather than represented by a core molecular function. Supporting Evidence: PMID:30266287 increased physical interaction of OSCP with Cyclophilin D (CypD) in AD cases |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MARK AS OVER ANNOTATED | Summary: Bare 'protein binding' from a reference binary interactome map. Uninformative molecular function term. Reason: Generic protein-binding annotation without functional specificity; retained per policy but flagged as uninformative. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | MARK AS OVER ANNOTATED | Summary: 'Protein binding' capturing the OSCP-huntingtin (HTT) interaction from a neurodegenerative-disease interactome. Uninformative molecular function term. Reason: Generic protein-binding annotation; the disease-interactome context does not confer a specific molecular function for OSCP. Retained per policy but flagged as uninformative. |
| GO:0009986 cell surface | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Orthology-transferred (rat) cell-surface localization, consistent with reports of an ecto-ATP synthase surface pool. This is a minor, non-canonical localization for a protein whose core function is at the mitochondrial inner membrane. Reason: A surface (ecto-ATP synthase) pool of OSCP has been reported, but this is a minor, non-core localization relative to the bulk mitochondrial-inner-membrane population. Supporting Evidence: PMID:17851741 associated to the plasma membrane |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Orthology-transferred (rat) ATP hydrolysis activity. The intact F1Fo complex can hydrolyze ATP as an artificial in vitro reverse reaction, but in vivo OSCP/Complex V only synthesizes ATP; this is not a physiological function of OSCP. Reason: UniProt states the complex in vivo can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Assigning ATP hydrolysis activity to OSCP over-represents a non-physiological reverse reaction of the whole complex; OSCP itself is non-catalytic. Supporting Evidence: PMID:12110673 The captured complex V displayed ATP hydrolysis activity that was |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Orthology-transferred protein-containing complex binding. OSCP is an integral subunit of the ATP synthase complex rather than a factor that binds a complex from outside; the part_of complex annotation captures this more accurately. Reason: OSCP is a constitutive structural subunit of Complex V, so 'complex binding' is a weak, generic descriptor that is better represented by its part_of proton-transporting ATP synthase complex membership. |
| GO:0045259 proton-transporting ATP synthase complex | IEA GO_REF:0000120 | ACCEPT | Summary: OSCP is a bona fide structural subunit of the proton-transporting ATP synthase complex. This is a core cellular-component annotation. Reason: Membership confirmed by immunocapture of the complete complex and by the cryo-EM structure, in which OSCP (chain O) is resolved within the peripheral stalk. Supporting Evidence: file:human/ATP5PO/ATP5PO-uniprot.txt a stationary peripheral stalk (subunits F6, b, d, and |
| GO:0071320 cellular response to cAMP | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Orthology-transferred (rat) response-to-cAMP process. Not a core, gene-specific function of a structural ATP synthase subunit. Reason: This process annotation was transferred from a rat ortholog and does not reflect a characterized OSCP-specific role; it over-annotates the gene's function. |
| GO:0071345 cellular response to cytokine stimulus | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Orthology-transferred (rat) response-to-cytokine process. Not a core, gene-specific function of a structural ATP synthase subunit. Reason: Transferred from a rat ortholog with no OSCP-specific mechanistic basis; over-annotates the gene relative to its established structural role in Complex V. |
| GO:1903924 estradiol binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Orthology-transferred (rat) estradiol-binding molecular function. There is no established estradiol-binding role for human OSCP as a structural stator subunit. Reason: This molecular function was transferred by Ensembl Compara from a rat ortholog and is not supported by any characterization of human OSCP function; it over-annotates the gene. |
| GO:0005743 mitochondrial inner membrane | NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep... | ACCEPT | Summary: ComplexPortal-curated mitochondrial inner membrane localization for the ATP synthase complex. Correct core location for OSCP. Reason: The ATP synthase holocomplex assembles in the mitochondrial inner membrane; OSCP is part of the peripheral (stator) stalk of that complex. Supporting Evidence: PMID:26297831 the stator casings fixed with the peripheral stator stalk |
| GO:0015986 proton motive force-driven ATP synthesis | NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep... | ACCEPT | Summary: ComplexPortal-curated involvement of the ATP synthase complex in proton motive force-driven ATP synthesis. Correct for OSCP as a subunit. Reason: OSCP is a required structural subunit of the complex that carries out proton motive force-driven ATP synthesis. Supporting Evidence: PMID:26297831 Mitochondrial ATP synthase is a motor enzyme in which a central shaft rotates in |
| GO:0045259 proton-transporting ATP synthase complex | NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep... | ACCEPT | Summary: ComplexPortal-curated membership of OSCP in the proton-transporting ATP synthase complex. Core cellular-component annotation. Reason: OSCP is a stator-stalk subunit of the assembled ATP synthase complex; complex assembly studies place it in the stator (b-e-g / peripheral stalk) machinery. Supporting Evidence: PMID:26297831 the stator casings fixed with the peripheral stator stalk |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: High-throughput mitochondrial-proteome localization. Consistent with OSCP being a mitochondrial protein; general term. Reason: OSCP is robustly detected in the high-confidence human mitochondrial proteome, consistent with all other localization evidence. Supporting Evidence: PMID:34800366 Quantitative high-confidence human mitochondrial proteome and its dynamics |
| GO:0045259 proton-transporting ATP synthase complex | IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: Direct experimental demonstration that OSCP is a subunit of immunocaptured human F1Fo ATP synthase. Core cellular-component annotation. Reason: Immunocapture of the intact complex identified OSCP among the subunits by specific antibodies and mass spectrometry, directly establishing complex membership. Supporting Evidence: PMID:12110673 subunits that were identified with specific antibodies against five of the |
| GO:0046933 proton-transporting ATP synthase activity, rotational mechanism | IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: OSCP contributes to the rotational ATP synthase activity of the immunocaptured complex, which displayed oligomycin-sensitive activity. Correct contributes_to usage for a structural subunit. Reason: The captured complex containing OSCP showed oligomycin-sensitive ATP synthase/hydrolase activity, and OSCP confers this oligomycin sensitivity; contributes_to appropriately reflects the non-catalytic structural contribution. Supporting Evidence: PMID:12110673 fully oligomycin and inhibitor protein IF(1)-sensitive |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-164832 | ACCEPT | Summary: Reactome-asserted inner-membrane localization (ATPase synthesizes ATP reaction). Correct core location. Reason: Reactome places OSCP with the ATP synthase in the mitochondrial inner membrane, consistent with structural and curated evidence. |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-164834 | ACCEPT | Summary: Reactome-asserted inner-membrane localization (enzyme-bound ATP release reaction). Correct core location. Reason: Consistent with OSCP's location in the inner-membrane ATP synthase complex. |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-164840 | ACCEPT | Summary: Reactome-asserted inner-membrane localization (ADP and Pi binding reaction). Correct core location. Reason: Consistent with OSCP's location in the inner-membrane ATP synthase complex. |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-8949580 | ACCEPT | Summary: Reactome-asserted inner-membrane localization (F1Fo ATP synthase dimerization). Correct core location. Reason: Consistent with OSCP's location in the inner-membrane ATP synthase complex. |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-9837978 | ACCEPT | Summary: Reactome-asserted inner-membrane localization (LONP1 binds inner-membrane proteins). Correct core location. Reason: Consistent with OSCP's location in the mitochondrial inner membrane. |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-9838004 | ACCEPT | Summary: Reactome-asserted inner-membrane localization (LONP1 degrades inner-membrane proteins). Correct core location. Reason: Consistent with OSCP's location in the mitochondrial inner membrane. |
| GO:0005739 mitochondrion | IDA PMID:15850986 Identification and validation of the mitochondrial F1F0-ATPa... | ACCEPT | Summary: Direct experimental mitochondrial localization from the study identifying OSCP as the target of the F1Fo-ATPase inhibitor Bz-423. General but correct. Reason: OSCP was studied as a mitochondrial F1Fo-ATPase component; mitochondrial localization is well supported. Supporting Evidence: PMID:15850986 sensitivity conferring protein (OSCP) component of the mitochondrial |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | KEEP AS NON CORE | Summary: Nuclear localization from a sperm-nucleus proteomics dataset. Almost certainly a mitochondrial-contaminant detection rather than a genuine nuclear function of a structural ATP synthase subunit. Reason: High-throughput sperm-nucleus proteomics can detect abundant mitochondrial proteins as contaminants; there is no functional evidence for a nuclear role of OSCP. Kept as non-core rather than removed, but not part of the core function. |
| GO:0005739 mitochondrion | HDA PMID:20833797 Phosphoproteome analysis of functional mitochondria isolated... | ACCEPT | Summary: Mitochondrial localization from a phosphoproteome analysis of isolated human muscle mitochondria. Correct general localization. Reason: OSCP was identified in purified functional mitochondria, consistent with its role as an inner-membrane ATP synthase subunit. |
| GO:0006754 ATP biosynthetic process | NAS PMID:17851741 IF(1) distribution in HepG2 cells in relation to ecto-F(0)F ... | ACCEPT | Summary: Author statement that OSCP is part of the ATP-synthesizing F0F1-ATP synthase. Correct but represented more specifically by proton motive force-driven mitochondrial ATP synthesis. Reason: ATP biosynthetic process is a correct parent process; the more specific GO:0042776 is the preferred core term, but this broader annotation is not wrong. Supporting Evidence: PMID:17851741 OSCP and beta subunits of F(0)F(1)ATPsynthase in HepG2 cells |
| GO:0042776 proton motive force-driven mitochondrial ATP synthesis | IMP PMID:15850986 Identification and validation of the mitochondrial F1F0-ATPa... | ACCEPT | Summary: Mutational/functional evidence (RNAi knockdown of OSCP altering cellular sensitivity to the OSCP-targeted F1Fo-ATPase inhibitor Bz-423) supporting OSCP involvement in mitochondrial ATP synthesis. This is a core biological process annotation. Reason: OSCP is directly implicated in F1Fo-ATPase function by the identification of OSCP as the Bz-423 target and by RNAi knockdown experiments, supporting its involvement in proton motive force-driven mitochondrial ATP synthesis. Supporting Evidence: PMID:15850986 expression using RNA interference and studying the sensitivity of these cells to |
| GO:0045259 proton-transporting ATP synthase complex | NAS PMID:7490082 Cloning of the cDNA for the human ATP synthase OSCP subunit ... | ACCEPT | Summary: Author statement (cDNA cloning paper) that ATP5O/OSCP is a key structural component of the ATP synthase stalk. Core cellular-component annotation. Reason: The cloning paper explicitly describes ATP5O as a key structural component of the stalk of the mitochondrial F1F0-ATP synthase, directly supporting complex membership. Supporting Evidence: PMID:7490082 This ATP5O subunit is a key structural component of the stalk of the mitochondrial respiratory chain |
| GO:1902600 proton transmembrane transport | NAS PMID:17851741 IF(1) distribution in HepG2 cells in relation to ecto-F(0)F ... | ACCEPT | Summary: Involvement in proton transmembrane transport as part of the F0F1-ATP synthase, which couples proton flux to ATP synthesis. Reasonable for OSCP as a subunit, though OSCP itself is in the peripheral stalk rather than the proton channel. Reason: The ATP synthase complex couples proton translocation across the inner membrane to ATP synthesis; OSCP is a required structural subunit of this proton-transporting complex. The annotation is appropriate at the complex level. Supporting Evidence: PMID:17851741 OSCP and beta subunits of F(0)F(1)ATPsynthase in HepG2 cells |
| GO:0005739 mitochondrion | IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: Direct mitochondrial localization from immunocapture of human F1Fo ATP synthase from heart and fibroblasts. General but correct. Reason: OSCP was co-purified with the intact mitochondrial ATP synthase complex, confirming mitochondrial localization. Supporting Evidence: PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of |
| GO:0005739 mitochondrion | IDA PMID:17851741 IF(1) distribution in HepG2 cells in relation to ecto-F(0)F ... | ACCEPT | Summary: Direct mitochondrial localization of OSCP in HepG2 cells. General but correct. Reason: OSCP is detected in mitochondria as an F0F1-ATP synthase subunit; the bulk pool is mitochondrial. Supporting Evidence: PMID:17851741 OSCP and beta subunits of F(0)F(1)ATPsynthase in HepG2 cells |
| GO:0005886 plasma membrane | IDA PMID:17851741 IF(1) distribution in HepG2 cells in relation to ecto-F(0)F ... | KEEP AS NON CORE | Summary: Plasma-membrane detection of OSCP as part of an ecto-F0F1-ATP synthase pool on HepG2 hepatocytes. A genuine but minor, non-canonical surface localization distinct from the core mitochondrial-inner-membrane role. Reason: The study reports OSCP associated with the plasma membrane as part of the reported cell-surface (ecto) ATP synthase; this is a minor surface pool and not the core inner-membrane function of OSCP. Supporting Evidence: PMID:17851741 associated to the plasma membrane |
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Download this section (compressed HTML)Q: Beyond its structural stator role, does OSCP acetylation at Lys-162 (regulated by SIRT3) or its interaction with cyclophilin D directly modulate ATP synthase output or permeability transition pore opening in vivo?
Experiment: Structure-guided mutagenesis of the OSCP F1-binding interface to quantify effects on coupling efficiency and oligomycin sensitivity in reconstituted human ATP synthase.
Experiment: Test whether the reported cell-surface (ecto) pool of OSCP reflects a genuine plasma-membrane targeting mechanism or mitochondrial contamination, using surface biotinylation combined with strict mitochondrial-contamination controls.
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