Function of CBFβ/Bro proteins

Adya, Neeraj; Castilla, Lucio H.; Liu, P.P

doi:10.1006/scdb.2000.0189

Cited by 61 publications

(63 citation statements)

References 46 publications

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“…Data represent results from a minimum of nine replicate samples and three separate studies with different culture preparations. specific 4 and varied by less than 10% in our studies.…”

Section: Fig 7 Runx2 Inhibits Steroid Activitycontrasting

confidence: 73%

“…The interaction between ER␣ and Stat5 also maps to the ER␣ DBD (71). Other transcriptional regulators seem to control Runx transcription factors by an interaction that requires, in whole or in part, the Runt domain (4,6,8,37,72), whereas ER␣ does not seem to associate in an efficient way with the Runt domain of Runx2 by itself (current study). As modeled in Fig.…”

Section: Fig 7 Runx2 Inhibits Steroid Activitymentioning

confidence: 63%

“…Consequently, changes in the balance of Runx2 and steroid hormone receptors in osteoblasts could integrate gene expression in complex but focused ways. For example, a high level of glucocorticoid could significantly limit development of the osteoblast phenotype in bone cells where Runx2 expression is evolving but 4 M. Centrella and T. L. McCarthy, unpublished observations.…”

Section: Fig 7 Runx2 Inhibits Steroid Activitymentioning

confidence: 99%

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Runx2 Integrates Estrogen Activity in Osteoblasts

McCarthy

Chang

Liu

et al. 2003

Journal of Biological Chemistry

108

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Steroids significantly effect skeletal integrity. For example, bone mass decreases with glucocorticoid excess or with estrogen depletion after menopause. Glucocorticoid suppresses gene expression by an essential skeletal tissue transcription factor, Runx2, in rat osteoblasts. We now report that estrogen enhances Runx2 activity in dose-and estrogen receptor-dependent ways independently of changes in Runx2 levels or its DNA binding potential. Estrogen receptor and Runx2 can be collected by co-immunoprecipitation. By two-hybrid gene expression analysis, high affinity complex formation involves portions of Runx2 outside of its own DNA binding domain and the DNA binding domain of the estrogen receptor. Consistent with this interaction, the stimulatory effect of estrogen on Runx2 activity is lost when the DNA binding domain of the estrogen receptor is eliminated. Unlike the stimulatory effect of estrogen and the inhibitory effect of glucocorticoid, androgen fails to increase Runx2 activity, whereas Runx2 potently suppresses gene expression induced by all three steroids. Finally, estrogen increases gene transcription by the transforming growth factor-␤ type I receptor gene promoter, which contains several Runx binding sequences, and enhances Smad dependent gene expression by transforming growth factor-␤ in osteoblasts. These results reveal that Runx2 can integrate complex effects on gene transcription in hormone-, growth factor-, and tissue-restricted ways.

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“…Data represent results from a minimum of nine replicate samples and three separate studies with different culture preparations. specific 4 and varied by less than 10% in our studies.…”

Section: Fig 7 Runx2 Inhibits Steroid Activitycontrasting

confidence: 73%

Section: Fig 7 Runx2 Inhibits Steroid Activitymentioning

confidence: 63%

Section: Fig 7 Runx2 Inhibits Steroid Activitymentioning

confidence: 99%

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Runx2 Integrates Estrogen Activity in Osteoblasts

McCarthy

Chang

Liu

et al. 2003

Journal of Biological Chemistry

108

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“…Both RUNX1 and LEF1 are DNA binding proteins, whose consensus binding sites have been determined (67,82,83). RUNX1 binding to DNA is through its central runt domain, and activation of the class I promoter depends on both its DNA binding and activation domains.…”

Section: Discussionmentioning

confidence: 99%

A T Lymphocyte-Specific Transcription Complex Containing RUNX1 Activates MHC Class I Expression

Howcroft

Weissman

Gégonne

et al. 2005

The Journal of Immunology

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MHC class I expression is subject to both tissue-specific and hormonal regulatory mechanisms. Consequently, levels of expression vary widely among tissues, with the highest levels of class I occurring in the lymphoid compartment, in T cells and B cells. Although the high class I expression in B cells is known to involve the B cell enhanceosome, the molecular basis for high constitutive class I expression in T cells has not been explored. T cell-specific genes, such as TCR genes, are regulated by a T cell enhanceosome consisting of RUNX1, CBFβ, LEF1, and Aly. In this report, we demonstrate that MHC class I gene expression is enhanced by the T cell enhanceosome and results from a direct interaction of the RUNX1-containing complex with the class I gene in vivo. T cell enhanceosome activation of class I transcription is synergistic with CIITA-mediated activation and targets response elements distinct from those targeted by CIITA. These findings provide a molecular basis for the high levels of MHC class I in T cells.

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“…CBF-b normally functions as a transcription factor for haematopoiesis, T-cell differentiation and bone development through binding with Runt-related transcription factors 1, 2 and 3 (RUNX1, 2 and 3) (Adya et al, 2000;de Bruijn & Speck, 2004;Ito, 2008). Structural studies have provided additional compelling evidence that CBF-b is an integral part of the HIV-1 Vif ubiquitin ligase complex (Guo et al, 2014;Kim et al, 2013).…”

mentioning

confidence: 99%

Vif determines the requirement for CBF-β in APOBEC3 degradation

Yoshikawa

Takeuchi

Yamada

et al. 2015

Journal of General Virology

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APOBEC3 (apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3) proteins are cellular DNA deaminases that restrict a broad spectrum of lentiviruses. This process is counteracted by Vif (viral infectivity factor) of lentiviruses, which binds APOBEC3s and promotes their degradation. CBF-b (core binding factor subunit b) is an essential co-factor for the function of human immunodeficiency virus type 1 Vif to degrade human APOBEC3s. However, the requirement for CBF-b in Vif-mediated degradation of other mammalian APOBEC3 proteins is less clear. Here, we determined the sequence of feline CBFB and performed phylogenetic analyses. These analyses revealed that mammalian CBFB is under purifying selection. Moreover, we demonstrated that CBF-b is dispensable for feline immunodeficiency virus Vif-mediated degradation of APOBEC3s of its host. These findings suggested that primate lentiviruses have adapted to use CBF-b, an evolutionary stable protein, to counteract APOBEC3 proteins of their hosts after diverging from other lentiviruses.

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Function of CBFβ/Bro proteins

Cited by 61 publications

References 46 publications

Runx2 Integrates Estrogen Activity in Osteoblasts

Runx2 Integrates Estrogen Activity in Osteoblasts

A T Lymphocyte-Specific Transcription Complex Containing RUNX1 Activates MHC Class I Expression

Vif determines the requirement for CBF-β in APOBEC3 degradation

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