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

ABSTRACT: Recent data have shown that Hypermethylated in cancer 1 (HIC1) is an important contributor to iTreg cell development and function. Using affinity-purification and tandem mass spectrometry we systematically characterized the HIC-1 interactome in human iTreg cells. On the basis of these data, we have shown that HIC1 is a part of FOXP3-RUNX1-CBFβ protein complex that regulates Treg signature genes and is indispensable for the suppressive function of FOXP3+ regulatory T cells. SRM was used to validate HIC1 interactors

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell, Cell Culture

SUBMITTER: Robert Moulder

LAB HEAD: Professor Riitta Lahesmaa

PROVIDER: PXD039337 | Pride | 2023-10-16

REPOSITORIES: Pride

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			Action	DRS
	190429_HIC1_24H_R1_1.raw	Raw
	190429_HIC1_24H_R1_2.raw	Raw
	190429_HIC1_24H_R1_3.raw	Raw
	190429_HIC1_24H_R2_1.raw	Raw
	190429_HIC1_24H_R2_2.raw	Raw

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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]

PMID: 37838026

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