Proteomics

Dataset Information

0

HIC1 interacts with FOXP3 multi protein complex: a novel mechanism to regulate human regulatory T cell differentiation and function


ABSTRACT: Transcriptional repressor, hypermethylated in cancer 1 (HIC1) is an important contributor to regulatory T (Treg) cell development and function. To investigate the mechanism by which it regulates Treg cell development, we systematically characterized the HIC1 interactome by affinity-purification mass spectrometry in human regulatory T cells. Interactors, involved in protein transport, mRNA processing, non-coding (ncRNA) transcription and RNA metabolism processes were identified. These data demonstrate that HIC1 is a part of a FOXP3-RUNX1-CBFβ protein complex that regulates Treg signature genes and is indispensable for the suppressive function of FOXP3+ regulatory T cells.

ORGANISM(S): Homo Sapiens

SUBMITTER: Robert Moulder  

PROVIDER: PXD038532 | panorama | Mon Oct 16 00:00:00 BST 2023

REPOSITORIES: PanoramaPublic

altmetric image

Publications

HIC1 interacts with FOXP3 multi protein complex: Novel pleiotropic mechanisms to regulate human regulatory T cell differentiation and function.

Andrabi Syed Bilal Ahmad SBA   Batkulwar Kedar K   Bhosale Santosh D SD   Moulder Robert R   Khan Meraj Hasan MH   Buchacher Tanja T   Khan Mohd Moin MM   Arnkil Ilona I   Rasool Omid O   Marson Alexander A   Kalim Ubaid Ullah UU   Lahesmaa Riitta R  

Immunology letters 20231012


Transcriptional repressor, hypermethylated in cancer 1 (HIC1) participates in a range of important biological processes, such as tumor repression, immune suppression, embryonic development and epigenetic gene regulation. Further to these, we previously demonstrated that HIC1 provides a significant contribution to the function and development of regulatory T (Treg) cells. However, the mechanism by which it regulates these processes was not apparent. To address this question, we used affinity-puri  ...[more]

Similar Datasets

2023-10-16 | PXD039337 | Pride
2019-01-08 | PRJEB27824 | EVA
| PRJNA412817 | ENA
| PRJNA1060707 | ENA
| PRJNA858820 | ENA
| PRJNA890656 | ENA
| PRJNA611580 | ENA
| PRJNA923391 | ENA
| PRJNA419354 | ENA
| PRJNA547593 | ENA