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Identification of PLP2 and RAB5C as novel TPD52 binding partners through yeast two-hybrid screening.
- Source :
-
Molecular biology reports [Mol Biol Rep] 2014 Jul; Vol. 41 (7), pp. 4565-72. Date of Electronic Publication: 2014 Mar 07. - Publication Year :
- 2014
-
Abstract
- Tumor protein D52 (TPD52) is overexpressed in different cancers, but its molecular functions are poorly defined. A large, low-stringency yeast two-hybrid screen using full-length TPD52 bait identified known partners (TPD52, TPD52L1, TPD52L2, MAL2) and four other preys that reproducibly bound TPD52 and TPD52L1 baits (PLP2, RAB5C, GOLGA5, YIF1A). PLP2 and RAB5 interactions with TPD52 were confirmed in pull down assays, with interaction domain mapping experiments indicating that both proteins interact with a novel binding region of TPD52. This study provides insights into TPD52 functions, and ways to maximise the efficiency of low-stringency yeast two-hybrid screens.
- Subjects :
- Binding Sites
Cell Line, Tumor
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Humans
MARVEL Domain-Containing Proteins chemistry
MARVEL Domain-Containing Proteins genetics
Neoplasm Proteins chemistry
Neoplasm Proteins genetics
Plasmids metabolism
Protein Binding
Protein Interaction Domains and Motifs
Protein Interaction Mapping
Proteolipids chemistry
Proteolipids genetics
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Transfection
Two-Hybrid System Techniques
rab5 GTP-Binding Proteins chemistry
rab5 GTP-Binding Proteins genetics
MARVEL Domain-Containing Proteins metabolism
Neoplasm Proteins metabolism
Proteolipids metabolism
Recombinant Fusion Proteins metabolism
rab5 GTP-Binding Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1573-4978
- Volume :
- 41
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Molecular biology reports
- Publication Type :
- Academic Journal
- Accession number :
- 24604726
- Full Text :
- https://doi.org/10.1007/s11033-014-3327-y