Document Detail


PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia.
MedLine Citation:
PMID:  8806687     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
M N Boddy; K Howe; L D Etkin; E Solomon; P S Freemont
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Oncogene     Volume:  13     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  1996 Sep 
Date Detail:
Created Date:  1996-11-05     Completed Date:  1996-11-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  971-82     Citation Subset:  IM    
Affiliation:
Protein Structure Laboratory, Imperial Cancer Research Fund, London, UK.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/U61397
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Amino Acid Sequence
Animals
Blotting, Northern
Blotting, Western
Cell Line
Clone Cells
Cloning, Molecular
Cyclin-Dependent Kinase Inhibitor p21
Cyclins / chemistry,  genetics*,  metabolism*
Escherichia coli / genetics,  metabolism
Fluorescent Antibody Technique, Indirect
Hela Cells / metabolism
Humans
Hybrid Cells
Lamins
Leukemia, Promyelocytic, Acute / genetics,  metabolism*,  pathology
Mice
Molecular Sequence Data
Neoplasm Proteins*
Nuclear Proteins / metabolism
Protein Biosynthesis
Recombinant Fusion Proteins / genetics,  metabolism
SUMO-1 Protein
Saccharomyces cerevisiae / genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Tissue Distribution
Transcription Factors / genetics,  metabolism*
Transfection
Tumor Cells, Cultured
Tumor Suppressor Proteins
Ubiquitins / chemistry,  genetics*,  metabolism
Chemical
Reg. No./Substance:
0/CDKN1A protein, human; 0/Cdkn1a protein, mouse; 0/Cyclin-Dependent Kinase Inhibitor p21; 0/Cyclins; 0/Lamins; 0/Neoplasm Proteins; 0/Nuclear Proteins; 0/Pml protein, mouse; 0/Recombinant Fusion Proteins; 0/SUMO-1 Protein; 0/Transcription Factors; 0/Tumor Suppressor Proteins; 0/Ubiquitins; 143220-95-5/PML protein, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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