The HIN-200 family: More than interferon-inducible genes?

Ludlow, Louise E.; Johnstone, Ricky W.; Clarke, Christopher J.

doi:10.1016/j.yexcr.2005.03.032

Cited by 158 publications

(168 citation statements)

References 93 publications

(152 reference statements)

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“…The HIN nomenclature describing their expression, IFN-induction, nuclear localization and characteristic 200-amino-acid domains was adopted. 21 MNDA is located on chromosome 1q22, before IFI16 and AIM2, and its protein contains a PAAD/DAPIN/Pyrin domain at its N-terminus, followed by a copy of a C-terminal 200A domain.…”

Section: Discussionmentioning

confidence: 99%

Identification of MNDA as a new marker for nodal marginal zone lymphoma

et al. 2009

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Clinical and biological studies on nodal marginal zone lymphoma (NMZL) are hampered by the lack of specific diagnostic markers and the low reproducibility of this diagnosis. A comparative expression-profiling study has shown a set of markers to be differentially expressed in NMZL compared with follicular lymphoma (FL), including myeloid cell nuclear differentiation antigen (MNDA), a nuclear protein expressed by myeloid cells and a subset of B-cells. The aim of this study was to characterize the expression of MNDA in normal and reactive human tissue, and in a large series of non-Hodgkin's B-cell lymphomas, with particular emphasis on NMZL and FL. Our results showed that MNDA is expressed in normal tissue by a subset of the marginal zone B cells. They also showed MNDA expression in subgroups of chronic lymphocytic leukemia, mantle-cell lymphoma, and diffuse large B-cell lymphoma, but MNDA was especially expressed by lymphomas derived from the marginal zone, such as mucosa-associated lymphoid-tissue lymphoma, splenic marginal-zone lymphoma and NMZL. MNDA expression was rarely observed in FL, a characteristic that is of potential value in distinguishing between NMZL and FL. MNDA expression is thus a useful tool for the recognition of NMZL.

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Section: Discussionmentioning

confidence: 99%

Identification of MNDA as a new marker for nodal marginal zone lymphoma

et al. 2009

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“…p204 is a member of the interferon-inducible murine p200 family proteins (Choubey et al, 1989;Deschamps et al, 2003;Ludlow et al, 2005). p204 consists of 640 amino acid (aa) residues.…”

Section: Introductionmentioning

confidence: 99%

“…Id proteins were identified to be the early response genes of BMP-2, -6, and -9 in a microarray, and they were found to quickly go down during the terminal differentiation of committed osteoblasts, suggesting that a balanced regulation of Id expression may be critical to BMP-induced osteoblast lineage-specific differentiation of mesenchymal stem cells (Ogata et al, 1993;Hollnagel et al, 1999;Amthor et al, 2002); however, the molecular mechanism by which Id proteins regulate osteogenesis remains unknown. p204 is a member of the interferon-inducible murine p200 family proteins (Choubey et al, 1989;Deschamps et al, 2003;Ludlow et al, 2005). p204 consists of 640 amino acid (aa) residues.…”

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confidence: 99%

p204 Protein Overcomes the Inhibition of Core Binding Factor α-1–mediated Osteogenic Differentiation by Id Helix-Loop-Helix Proteins

Luan

Yang

et al. 2008

MBoC

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Id proteins play important roles in osteogenic differentiation; however, the molecular mechanism remains unknown. In this study, we established that inhibitor of differentiation (Id) proteins, including Id1, Id2, and Id3, associate with core binding factor ␣-1 (Cbfa1) to cause diminished transcription of the alkaline phosphatase (ALP) and osteocalcin (OCL) gene, leading to less ALP activity and osteocalcin (OCL) production. Id acts by inhibiting the sequence-specific binding of Cbfa1 to DNA and by decreasing the expression of Cbfa1 in cells undergoing osteogenic differentiation. p204, an interferon-inducible protein that interacts with both Cbfa1 and Id2, overcame the Id2-mediated inhibition of Cbfa1-induced ALP activity and OCL production. We show that 1) p204 disturbed the binding of Id2 to Cbfa1 and enabled Cbfa1 to bind to the promoters of its target genes and 2) that p204 promoted the translocation from nucleus to the cytoplasm and accelerated the degradation of Id2 by ubiquitin-proteasome pathway during osteogenesis. Nucleus export signal (NES) of p204 is required for the p204-enhanced cytoplasmic translocation and degradation of Id2, because a p204 mutant lacking NES lost these activities. Together, Cbfa1, p204, and Id proteins form a regulatory circuit and act in concert to regulate osteoblast differentiation. INTRODUCTIONThe differentiation of uncommitted mesenchymal cells to osteoblasts is a fundamental process in embryonic development and bone repair. The bone morphogenetic proteins (BMPs) are important regulators of this process (Heldin et al., 1997;Miyazono et al., 2000). They function by binding cell surface receptors; signaling by Smad proteins; and activating bone-specific genes, including core binding factor ␣-1 (Cbfa1) (Ducy, 2000;Miyazono et al., 2001;Attisano and Wrana, 2002). This process is positively or negatively regulated by a variety of coactivators and corepressors (Ducy et al., 2000;Miyazono et al., 2001;Attisano and Wrana, 2002). Cbfa1, also known as Runx2, PeBP2␣A, Osf2, or AML3, is a member of the runt family of transcription factors. It is an essential transcription factor of osteoblast and bone formation (Ducy, 2000). During skeletal development, Cbfa1 is observed first in early mesenchymal condensations, and it is then principally expressed in osteoblasts . Cbfa1 Ϫ/Ϫ mice exhibit a complete lack of ossification, and they die immediately after birth (Komori et al., 1997). Cbfa1 maintains osteoblastic function by regulating the expression of several bone-specific genes such as osteopontin and osteocalcin and by controlling bone extracellular matrix deposition (Ducy, 2000). Mutations in Cbfa1 are found in 65-80% of individuals with cleidocranial dysplasia (CCD) (Lee et al., 1997;Mundlos and Olsen, 1997;Zhou et al., 1999). The molecular mechanisms underlying the pathogenesis of CCD are not completely defined. Some mutations of Cbfa1 abolish its DNA binding activity (Lee et al., 1997;Zhou et al., 1999) and others disturb the association of Cbfa1 to its binding partners, including Sma...

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“…The PYD domain (also known as DAPIN or PAAD domain) belongs to the death domain superfamily and is an alpha-helical motif that forms homotypic interactions with other PYD containing proteins. The 200 amino acid DNA binding HIN domain is classified into three subtypes, termed A, B and C, based on consensus motifs [8]. POP3, the most recent member of this gene cluster to be identified, lacks the HIN domains found in other PYHIN proteins [3].…”

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confidence: 99%