|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
24
|
|
pubmed:dateCreated |
1999-7-6
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Using a yeast two-hybrid screening strategy with a common tumour-derived p53 mutant as bait, we identified several mutant p53-interacting partners including the known proteins wild-type (wt) p53, hUBC9 and GBP/PIAS1. In addition, a novel protein partner was identified which we have termed MBP1, for Mutant p53-Binding Protein 1. MBP1 is a new member of the emerging fibulin gene family, which currently comprises fibulin-1, fibulin-2 and S1-5. Expression of MBP1 mRNA is differentially regulated both temporally during development of the mouse embryo and in a tissue-specific manner within the adult. Specific interaction between MBP1 and mutant p53 was illustrated by both two-hybrid analysis in yeast and co-immunoprecipitation in mammalian cells. MBP1 displayed the following order of binding specificity towards different p53 forms: H175 > G281 > H273 > or = W248>wt p53. Thus, MBP1 appears to bind preferentially to p53 mutants of the 'structural' rather than 'contact' class, reflecting a potential bias towards those mutants having a significant alteration in conformation from that assumed by wt p53. We propose that MBP1 is the product of a candidate oncogene as rates of both neoplastic transformation and tumour cell growth were shown to be significantly enhanced when the protein is ectopically overexpressed. Furthermore, MBP1 may play a role in determining if a 'gain of function' effect is seen with certain p53 mutants.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
0950-9232
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
17
|
|
pubmed:volume |
18
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
3608-16
|
|
pubmed:dateRevised |
2007-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10380882-Amino Acid Sequence,
pubmed-meshheading:10380882-Animals,
pubmed-meshheading:10380882-Calcium-Binding Proteins,
pubmed-meshheading:10380882-Cell Division,
pubmed-meshheading:10380882-Cell Transformation, Neoplastic,
pubmed-meshheading:10380882-Cloning, Molecular,
pubmed-meshheading:10380882-Embryo, Mammalian,
pubmed-meshheading:10380882-Extracellular Matrix Proteins,
pubmed-meshheading:10380882-Gene Expression Regulation, Developmental,
pubmed-meshheading:10380882-Humans,
pubmed-meshheading:10380882-Mice,
pubmed-meshheading:10380882-Molecular Sequence Data,
pubmed-meshheading:10380882-Mutation,
pubmed-meshheading:10380882-Oncogene Proteins,
pubmed-meshheading:10380882-Organ Specificity,
pubmed-meshheading:10380882-Protein Binding,
pubmed-meshheading:10380882-Protein Conformation,
pubmed-meshheading:10380882-RNA, Messenger,
pubmed-meshheading:10380882-Sequence Deletion,
pubmed-meshheading:10380882-Sequence Homology, Amino Acid,
pubmed-meshheading:10380882-Tumor Cells, Cultured,
pubmed-meshheading:10380882-Tumor Suppressor Protein p53,
pubmed-meshheading:10380882-Yeasts
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
MBP1: a novel mutant p53-specific protein partner with oncogenic properties.
|
|
pubmed:affiliation |
Oncology Department, Rhône-Poulenc Rorer, CRVA, Vitry-sur-Seine, France.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
