Proteomics

Dataset Information

0

Identification of TI-4-interacting proteins


ABSTRACT: Transcriptional co-activator with PDZ-binding motif (TAZ) (the official gene name; WWTR1) interacts with transcription factors in the nucleus but when phosphorylated, translocates to the cytoplasm and undergoes degradation. Chemical compounds that modulate the subcellular localization of TAZ are supposed to activate or inhibit TAZ. We identified a compound that shifts TAZ to the cytoplasm independently of phosphorylation and named it TI-4. We used affinity beads and obtained as a putative target of TI-4 Chromosomal Segregation 1 Like (CSE1L), which is involved in the recycling of importin alpha and is known as a biomarker of cancer malignancy.

INSTRUMENT(S): maXis

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

DISEASE(S): Brain Glioblastoma Multiforme

SUBMITTER: Junichi MARUYAMA  

LAB HEAD: Yutaka HATA

PROVIDER: PXD024194 | Pride | 2021-09-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
analysis_90K.baf Other
analysis_90K.mgf Mgf
analysis_90K.mzid.gz Mzid
Items per page:
1 - 3 of 3
altmetric image

Publications

CSE1L promotes nuclear accumulation of transcriptional coactivator TAZ and enhances invasiveness of human cancer cells.

Nagashima Shunta S   Maruyama Junichi J   Honda Kaori K   Kondoh Yasumitsu Y   Osada Hiroyuki H   Nawa Makiko M   Nakahama Ken-Ichi KI   Ishigami-Yuasa Mari M   Kagechika Hiroyuki H   Sugimura Haruhiko H   Iwasa Hiroaki H   Arimoto-Matsuzaki Kyoko K   Nishina Hiroshi H   Hata Yutaka Y  

The Journal of biological chemistry 20210520 1


The transcriptional coactivator with PDZ-binding motif (TAZ) (WWTR1) induces epithelial-mesenchymal transition and enhances drug resistance in multiple cancers. TAZ has been shown to interact with transcription factors in the nucleus, but when phosphorylated, translocates to the cytoplasm and is degraded through proteasomes. Here, we identified a compound TAZ inhibitor 4 (TI-4) that shifted TAZ localization to the cytoplasm independently of its phosphorylation. We used affinity beads to ascertai  ...[more]

Similar Datasets

2014-09-22 | PXD000892 | Pride
2022-08-31 | GSE197987 | GEO
2020-11-18 | GSE161611 | GEO
| PRJNA635221 | ENA
| PRJNA989666 | ENA
2023-06-01 | GSE153558 | GEO
2009-06-15 | E-GEOD-11835 | biostudies-arrayexpress
| PRJNA813298 | ENA
| PRJNA993464 | ENA
2010-01-22 | E-GEOD-19753 | biostudies-arrayexpress