| http://purl.uniprot.org/citations/32866687 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32866687 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32866687 | http://www.w3.org/2000/01/rdf-schema#comment | "Human caseinolytic peptidase B protein homolog (CLPB), also known as suppressor of potassium transport defect 3 (SKD3), is a broadly-expressed member of the family of ATPases associated with diverse cellular activities (AAA+). Mutations in the human CLPB gene cause 3-methylglutaconic aciduria type VII. CLPB is upregulated in acute myeloid leukemia (AML), where it contributes to anti-cancer drug resistance. The biological function of CLPB in human cells and mechanistic links to the clinical phenotypes are currently unknown. Herein, subcellular fractionation of human HEK-293 and BT-549 cells showed that a single 57-kDa form of CLPB was present in the mitochondria and not in the cytosolic fraction. Immunofluorescence staining of HEK-293 and BT-549 cells with anti-CLPB antibody co-localized with the mitochondrial staining using a MitoTracker dye. In purified intact mitochondria, CLPB was protected against externally added proteinase K, but it was susceptible to degradation after disruption of the outer membrane, indicating that CLPB resides in the mitochondrial intermembrane space. Overexpressed CLPB, while properly trafficked to the mitochondria, appeared to form large clusters/aggregates that were resistant to extraction with non-ionic detergents and were readily visualized by immunofluorescence microscopy. Importantly, endogenous CLPB formed high molecular weight protein complexes in an ATP-dependent manner that were detected by blue native polyacrylamide gel electrophoresis. These results demonstrate that ATP induces a structural change in CLPB and controls its ability to self-associate or form complexes with other proteins in the intermembrane space of mitochondria."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biocel.2020.105841"xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biocel.2020.105841"xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/author | "Zolkiewski M."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/author | "Zolkiewski M."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/author | "Zolkiewska A."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/author | "Zolkiewska A."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/author | "Thevarajan I."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/author | "Thevarajan I."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/name | "Int. J. Biochem. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/name | "Int. J. Biochem. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/pages | "105841"xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/pages | "105841"xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/title | "Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/title | "Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space."xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/volume | "127"xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://purl.uniprot.org/core/volume | "127"xsd:string |
| http://purl.uniprot.org/citations/32866687 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32866687 |
| http://purl.uniprot.org/citations/32866687 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32866687 |
| http://purl.uniprot.org/citations/32866687 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/32866687 |
| http://purl.uniprot.org/citations/32866687 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/32866687 |