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Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Am+J+Physiol+Cell+Physiol 2014 ; 306 (9): C805-18 Nephropedia Template TP
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Label-free quantitative proteomic analysis of the YAP/TAZ interactome #MMPMID24573087
Am J Physiol Cell Physiol 2014[May]; 306 (9): C805-18 PMID24573087show ga
The function of an individual protein is typically defined by protein-protein interactions orchestrating the formation of large complexes critical for a wide variety of biological processes. Over the last decade the analysis of purified protein complexes by mass spectrometry became a key technique to identify protein-protein interactions. We present a fast and straightforward approach for analyses of interacting proteins combining a Flp-in single-copy cellular integration system and single-step affinity purification with single-shot mass spectrometry analysis. We applied this protocol to the analysis of the YAP and TAZ interactome. YAP and TAZ are the downstream effectors of the mammalian Hippo tumor suppressor pathway. Our study provides comprehensive interactomes for both YAP and TAZ and does not only confirm the majority of previously described interactors but, strikingly, revealed uncharacterized interaction partners that affect YAP/TAZ TEAD-dependent transcription. Among these newly identified candidates are Rassf8, thymopoetin, and the transcription factors CCAAT/enhancer-binding protein (C/EBP)beta/delta and core-binding factor subunit beta (Cbfb). In addition, our data allowed insights into complex stoichiometry and uncovered discrepancies between the YAP and TAZ interactomes. Taken together, the stringent approach presented here could help to significantly sharpen the understanding of protein-protein networks.
|*Protein Interaction Mapping/methods[MESH]
|*Protein Interaction Maps[MESH]
|*Proteomics/methods[MESH]
|Acyltransferases[MESH]
|Adaptor Proteins, Signal Transducing/genetics/*metabolism[MESH]