Dataset Information

Mouse CD4+ T cells IP-MS - Reversing SKI-SMAD4-mediated suppression is essential for TH17 cell differentiation

ABSTRACT: Identifying Smad4-binding proteins in mouse CD4+ T cells under IL6SB condition. Mouse CD4+ T cells were isolated from mouse spleen and lymph nodes.

OTHER RELATED OMICS DATASETS IN: PRJNA394763PRJNA394907

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Spleen, T Cell, Lymph Node

SUBMITTER: Yisong Wan

LAB HEAD: Yisong Wan

PROVIDER: PXD007172 | Pride | 2017-10-26

REPOSITORIES: Pride

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			Action	DRS
	QK041415_SZ_IP_1.raw	Raw
	QK041415_SZ_IP_10.raw	Raw
	QK041415_SZ_IP_10_150417203411.raw	Raw
	QK041415_SZ_IP_11.raw	Raw
	QK041415_SZ_IP_11_150415235956.raw	Raw

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Reversing SKI-SMAD4-mediated suppression is essential for TH17 cell differentiation.

Zhang Song S Takaku Motoki M Zou Liyun L Gu Ai-di AD Chou Wei-Chun WC Zhang Ge G Wu Bing B Kong Qing Q Thomas Seddon Y SY Serody Jonathan S JS Chen Xian X Xu Xiaojiang X Wade Paul A PA Cook Donald N DN Ting Jenny P Y JPY Wan Yisong Y YY

Nature 20171025 7678

T helper 17 (TH17) cells are critically involved in host defence, inflammation, and autoimmunity. Transforming growth factor β (TGFβ) is instrumental in TH17 cell differentiation by cooperating with interleukin-6 (refs 6, 7). Yet, the mechanism by which TGFβ enables TH17 cell differentiation remains elusive. Here we reveal that TGFβ enables TH17 cell differentiation by reversing SKI-SMAD4-mediated suppression of the expression of the retinoic acid rece ...[more]

PMID: 29072299

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Project description:We defined the RARα interactome in the MDA-MB453 breast cancer cell line genetically engineered to over-express an N-terminally tagged version of the nuclear retinoic acid receptor. Twenty eight nuclear proteins which interact with RARα and whose interaction is stimulated or reduced by the pan-RAR ligand, all-trans retinoic acid (ATRA) were identified. Given the potential significance of the S100A3 calcium-binding protein in the control of tumor progression, we focused our attention on this factor. Using the two models represented by the ATRA-sensitive SKBR3 and MCF7 breast cancer cell lines characterized by constitutive expression of S100A3 and RARα, we demonstrate that the endogenous forms of S100A3 and RARα interact in physiological conditions. The interaction of S100A3 with RARα is cell context independent and it is observed not only in breast cancer but also in acute promyelocytioc leukemia (APL) cells, characterized by expression of the RARα-derived PML-RARα oncogene, which is the product of the t(15:17) chromosomal translocation. S100A3 interacts directly and specifically with RARα and PML-RARα, being unable to bind other members of the RAR/RXR family of retinoid nuclear receptors. The interaction surface maps to the carboxyl-terminal region of the RARα ligand binding domain. Binding of S100A3 to RARα and PML-RARα controls the constitutive and ATRA-dependent degradation of the two receptors. Silencing of the S100A3 gene decreases the amounts of RARα in breast SK-BR-3 and lung A549 cancer cells, rendering them more refractory to the anti-proliferative action of ATRA. In SK-BR-3 cells, this effect is accompanied by a decrease in the lactogenic/differentiating action of ATRA. In APL-derived NB4 cells, S100A3 knock-down reduces the amounts of both RARα and PML-RARα. Contemporaneous down-regulation of the two receptors is associated with an increase in the basal and ATRA-induced expression of many granulocytic differentiation markers. Opposite on RARα and PML-RARα levels as well as ATRA induced differentiation markers are observed upon over-expression of S100A3 in NB4 cells.

Dataset Information

Mouse CD4+ T cells IP-MS - Reversing SKI-SMAD4-mediated suppression is essential for TH17 cell differentiation

Dataset's files

Publications

Reversing SKI-SMAD4-mediated suppression is essential for T<sub>H</sub>17 cell differentiation.

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