Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects

Berthet, Cyril; Guéhenneux, Fabienne; Revol, Valérie; Samarut, C; Lukaszewicz, Agnès; Dehay, Colette; Dumontet, Charles; Magaud, Jean‐Pierre; Rouault, Jean‐Pierre

doi:10.1046/j.1356-9597.2001.00497.x

Cited by 81 publications

(94 citation statements)

References 46 publications

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“…However, we failed to observe any potentiation of TRa/BTG1 transcriptional activity by PRMT1 coexpression, in agreement with inability of BTG1 to interact with PRMT1 in the presence of TRa (data not shown). We obtained similar data indicating that PRMT1 does not affect CMD1/ BTG1 transcriptional activity, a result well supported by the observation that PRMT1 and CMD1 recognize a common BTG1 sequence (C box; Berthet et al, 2002;present data), thus precluding an interaction including the three proteins. In addition, in these experiments, we unexpectedly found that PRMT1 is probably to be considered as a CMD1 coactivator.…”

Section: Btg1 Is a Coactivator Of Positive Regulators Of Myoblast Difsupporting

confidence: 72%

“…Instead, we found that the BTG1 A box, a well-conserved sequence in all members of the BTG family, with an unknown function prior to this study, interacts both with TRa1 and CMD1. In addition, whereas the C box, already shown to interact with PRMT1 (Berthet et al, 2002), is specifically involved in the physical interaction with CMD1, the 129-171 BTG1 C-terminus interacts with TRa1. Therefore, recruitment of various transcription factors by BTG1 involves several domains of the protein.…”

Section: Btg1 Is a Coactivator Of Positive Regulators Of Myoblast Difmentioning

confidence: 99%

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Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

et al. 2005

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The btg1 (B-cell translocation gene 1) gene coding sequence was isolated from a translocation break point in a case of B-cell chronic lymphocytic leukaemia. We have already shown that BTG1, considered as an antiproliferative protein, strongly stimulates myoblast differentiation. However, the mechanisms involved in this influence remained unknown. In cultured myoblasts, we found that BTG1 stimulates the transcriptional activity of nuclear receptors (T3 and all-trans retinoic acid receptors but not RXRa and PPARc), c-Jun and myogenic factors (CMD1, Myf5, myogenin). Immunoprecipitation experiments performed in cells or using in vitro-synthesized proteins and GST pull-down assays established that BTG1 directly interacts with T3 and all-trans retinoic acid receptors and with avian MyoD (CMD1). These interactions are mediated by the transactivation domain of each transcription factor and the A box and C-terminal part of BTG1. NCoR presence induces the ligand dependency of the interaction with nuclear receptors. Lastly, deletion of BTG1 interacting domains abrogates its ability to stimulate nuclear receptors and CMD1 activity, and its myogenic influence. In conclusion, BTG1 is a novel important coactivator involved in the regulation of myoblast differentiation. It not only stimulates the activity of myogenic factors, but also of nuclear receptors already known as positive myogenic regulators.

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Section: Btg1 Is a Coactivator Of Positive Regulators Of Myoblast Difsupporting

confidence: 72%

Section: Btg1 Is a Coactivator Of Positive Regulators Of Myoblast Difmentioning

confidence: 99%

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

et al. 2005

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“…First, TIS21 interacts with protein-arginine N-methyltransferase (PRMT1, Lin et al 1996;Berthet et al 2002) and it acts as a substrate of arginine methyltransferase (Lim et al 1998b). BTG2 /TIS21 also interacts with murine homolog of yeast CAF1 protein (Rouault et al 1998), homeoprotein Hoxb9 (Prevot et al 2000) and hCAF1/hPOP2 (Prevot et al 2001).…”

Section: Proteins Interacting With Tis21mentioning

confidence: 99%

TIS21 /BTG2/PC3 as a link between ageing and cancer: cell cycle regulator and endogenous cell death molecule

Lim

2006

J Cancer Res Clin Oncol

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TIS21/BTG2/PC3 , orthologs of mouse, human and rat, respectively, is initially identified as one of the early growth response genes and induced by various stimulations. TIS21 belongs to antiproliferative (APRO) gene family containing the BTG-Box A (Y 50 -N 71 ) and BTG-Box B (L 97 -E 115 ), which are highly conserved among various species. On the other hand, it has lately been found that the expression of TIS21 is constitutive and high in thymus, lung alveolar epithelium, proximal tubule of kidney and basal cell layer of prostate acini. Potential roles of TIS21 have been suggested as transcriptional co-regulator, differentiation and antiapoptotic factor in neurogenesis, key mediator of the stagespecific expansion of thymocyte and negative regulator of hematopoietic progenitor expansion, and tumor suppressor gene in both mouse and human. In addition, as pan-cell cycle regulator TIS21 induces G1/S arrest by pRB dependently and pRB independently and G2/M arrest and cell death in the p53 null tumor cells, and regulates the development of vertebrate patterning in mouse, paraxial mesoderm development in zebrafish, and notochord development in Xenopus. It has been known that the expression of TIS21 depends on the induction of wt p53 when cells are damaged, however, it can also be upregulated p53 independently by the activation of PKC-d pathway in tumor cells. The characteristic roles of TIS21 are discussed in the present review: (1) TIS21 inhibits early phase of carcinogenesis in its high expressers such as kidney, prostate, breast and thymus: Loss of constitutive and high expression of TIS21 was observed in the precancerous lesions as well as tumor tissues. As an endogenous cell death molecule, TIS21 may be involved in translocation of Pin-1 to cytoplasm. Pin-1 subsequently interacts with Serine 147 residue in TIS21 protein, resulting in mitochondrial depolarization. (2) TIS21 regulates transition of cell cycle at G1/S and G2/M phases in cancer cells with inactive pRB and/or p53, as well as in normal cells by regulating pRB/p16INK4a pathway. The latter has already been well elucidated; TIS21 inhibits the expression of cyclin D1, thus resulting in the arrest of cells at G1/S phase by pRB and p53 dependent manner. On the other hand, TIS21 inhibits degradations of cyclin A and cyclin B1 at G2/M phase, and directly binds to Cdc2, resulting in the failure of mitotic exit and then increasing the tumor cell death, when stimulated by high concentration of EGF. Therefore, TIS21 can be suggested as a pan-cell cycle modulator. (3) TIS21 regulates embryo development by activating BMP signal through interaction with Smad 1 and Smad 8, thereby regulating vertebral patterning in mice. It is also involved in notochord development in Xenopus and paraxial mesoderm development in zebrafish. Based on the previous report that the expression of TIS21 is involved in the induction of senescence after chemotherapy of cancer cells, which can be a mechanism to resist carcinogenesis, TIS21 /BTG2/ PC3 , the endogenous cell death mol...

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“…In addition, both Btg1 and Btg2 proteins have been shown to interact with and stimulate the activity of protein arginine methyltransferase-1 (PRMT1), the major arginine methyltransferase in mammals (Lin et al, 1996;Berthet et al, 2002). Protein arginine methylation is an emergent posttranslational modification involved in a growing number of cellular processes, including transcriptional regulation, cell signaling, DNA repair, and RNA processing (Robin-Lespinasse et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Btg1 and Btg2 gene expression during early chick development

Kamaid

Giráldez

2008

Developmental Dynamics

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Btg/Tob genes encode for a new family of proteins with antiproliferative functions, which are also able to stimulate cell differentiation. Btg1 and Btg2 are the most closely related members in terms of gene sequence. We analyzed their expression patterns in avian embryos by in situ hybridization, from embryonic day 1 to 3. Btg1 was distinctively expressed in the Hensen's node, the notochord, the cardiogenic mesoderm, the lens vesicle, and in the apical ectodermal ridge and mesenchyme of the limb buds. On the other hand, Btg2 expression domains included the neural plate border, presomitic mesoderm, trigeminal placode, and mesonephros. Both genes were commonly expressed in the myotome, epibranchial placodes, and dorsal neural tube. The results suggest that Btg1 and Btg2 are involved in multiple developmental processes. Overlapping expression of Btg1 and Btg2 may imply redundant functions, but unique expression patterns suggest also differential regulation and function.

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Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects

Abstract: Background : Several recent reports have connected protein methylation with differentiation. Furthermore, the BTG/TOB proteins have also been implicated in such control. BTG1 and 2 have been shown to interact with PRMT1 (predominant cellular arginine N-methyltransferase of type I).

Cited by 81 publications

References 46 publications

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

Coactivation of nuclear receptors and myogenic factors induces the major BTG1 influence on muscle differentiation

TIS21 /BTG2/PC3 as a link between ageing and cancer: cell cycle regulator and endogenous cell death molecule

Btg1 and Btg2 gene expression during early chick development

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