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rdf:type |
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lifeskim:mentions |
umls-concept:C0023487,
umls-concept:C0205314,
umls-concept:C0449432,
umls-concept:C0679622,
umls-concept:C0751283,
umls-concept:C0949455,
umls-concept:C1179435,
umls-concept:C1366903,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248
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pubmed:issue |
5
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pubmed:dateCreated |
1996-11-5
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pubmed:databankReference |
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pubmed:abstractText |
Acute promyelocytic leukaemia (APL) arises following a reciprocal translocation t(15;17) that fuses PML with retinoic acid receptor alpha (RARA). The PML-RARA fusion protein targets and disrupts nuclear multiprotein complexes called PODs, ND10 or NBs, a process which is associated with a block in myeloid differentiation leading to APL. A human B-cell cDNA library was screened for PML-interacting clones and a single positive clone (PIC1) was isolated. The sequence of PIC1 shows 52% identity to a S. cerevisiae ubiquitin-like protein that was cloned as a suppressor of mutations in MIF2, a protein required for mitotic spindle integrity during anaphase. Transient transfection of NIH3T3 cells with PIC1 results in a nuclear staining pattern coincident with that of endogenous mouse PML. Further, cotransfection of PIC1 with human PML produces a completely overlapping staining pattern between the two proteins. An antibody raised against PIC1 detects a punctate staining pattern in HeLa cells that is coincident with endogenous human PML. There is no significant colocalisation observed between the staining of PML/ PML-RARA and PIC1 in an APL-derived cell line NB4, as compared to cells expressing only wild type PML. However, following all trans retinoic acid treatment of NB4 cells a significant relocalisation of PIC1 and PML is observed. PIC1 is the first identified NB-associated protein that interacts with PML, the function of which may lead to a fuller understanding of the molecular events leading to APL.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDKN1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/Lamins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pml protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
971-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8806687-3T3 Cells,
pubmed-meshheading:8806687-Amino Acid Sequence,
pubmed-meshheading:8806687-Animals,
pubmed-meshheading:8806687-Blotting, Northern,
pubmed-meshheading:8806687-Blotting, Western,
pubmed-meshheading:8806687-Cell Line,
pubmed-meshheading:8806687-Clone Cells,
pubmed-meshheading:8806687-Cloning, Molecular,
pubmed-meshheading:8806687-Cyclin-Dependent Kinase Inhibitor p21,
pubmed-meshheading:8806687-Cyclins,
pubmed-meshheading:8806687-Escherichia coli,
pubmed-meshheading:8806687-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:8806687-HeLa Cells,
pubmed-meshheading:8806687-Humans,
pubmed-meshheading:8806687-Hybrid Cells,
pubmed-meshheading:8806687-Lamins,
pubmed-meshheading:8806687-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:8806687-Mice,
pubmed-meshheading:8806687-Molecular Sequence Data,
pubmed-meshheading:8806687-Neoplasm Proteins,
pubmed-meshheading:8806687-Nuclear Proteins,
pubmed-meshheading:8806687-Protein Biosynthesis,
pubmed-meshheading:8806687-Recombinant Fusion Proteins,
pubmed-meshheading:8806687-SUMO-1 Protein,
pubmed-meshheading:8806687-Saccharomyces cerevisiae,
pubmed-meshheading:8806687-Sequence Analysis, DNA,
pubmed-meshheading:8806687-Sequence Homology, Amino Acid,
pubmed-meshheading:8806687-Tissue Distribution,
pubmed-meshheading:8806687-Transcription Factors,
pubmed-meshheading:8806687-Transfection,
pubmed-meshheading:8806687-Tumor Cells, Cultured,
pubmed-meshheading:8806687-Tumor Suppressor Proteins,
pubmed-meshheading:8806687-Ubiquitins
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pubmed:year |
1996
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pubmed:articleTitle |
PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia.
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pubmed:affiliation |
Protein Structure Laboratory, Imperial Cancer Research Fund, London, UK.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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