The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation?

Stec, Ingrid; Nagl, Sylvia; Ommen, Gert‐Jan B. van; Dunnen, Johan T. den

doi:10.1016/s0014-5793(00)01449-6

Cited by 203 publications

(186 citation statements)

References 22 publications

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“…Lens epithelial cell‐derived growth factor plays an important role in tethering HIV‐1 cDNA to human chromatin through the PWWP domain (Blokken et al ., 2017). Disruption of the PWWP domain of the WHSC1 protein results in lymphoid multiple myeloma(Stec et al ., 2000). The S144I mutation in the PWWP domain of mismatch repair protein 6 leads to hereditary nonpolyposis colorectal cancer(Laguri et al ., 2008).…”

Section: Discussionmentioning

confidence: 99%

Role of hepatoma‐derived growth factor in promoting de novo lipogenesis and tumorigenesis in hepatocellular carcinoma

et al. 2018

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Although identified as a growth factor, the mechanism by which hepatoma‐derived growth factor (HDGF) promotes cancer development remains unclear. We found that nuclear but not cytoplasmic HDGF is closely associated with prognosis of hepatocellular carcinoma (HCC). RNA‐sequencing analysis further demonstrated that the nuclear role of HDGF involved regulation of transcription of lipid metabolism genes. HDGF‐induced expression of lipogenic genes was mainly associated with activation of sterol regulatory element binding protein (SREBP) transcription factor. Coexpression of SREBP‐1 and nuclear HDGF predicts poor prognosis for HCC. In addition, by changing the first amino acid of the PWWP domain from proline to alanine, the type of PWWP domain changed from P‐ to A‐type, resulting in inability to induce SREBP‐1‐mediated gene transcription. The type of PWWP domain affects the recruitment of the C‐terminal binding protein‐1 transcriptional repressor on the promoter of the lipogenic gene. Our data indicate that HDGF acts as a coactivator of SREBP1‐mediated transcription of lipogenic genes. The PWWP domain is crucial for HDGF to promote lipogenesis. Moreover, transcriptional regulation of nuclear HDGF plays important roles in the development of HCC.

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Section: Discussionmentioning

confidence: 99%

Role of hepatoma‐derived growth factor in promoting de novo lipogenesis and tumorigenesis in hepatocellular carcinoma

et al. 2018

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“…There are two dominant elements, a "PWWP domain" (residues 1-93) and an AT-Hook pair ( 178 PKRGRPAATEVKIPKPRGRPK 198 ). The PWWP domain is found in numerous other nuclear proteins [134,135]. Deletion of this domain or just its beta-barrel sub-domain from p75 disrupts microscopically detectable tethering to condensed chromosomes [93].…”

Section: Structure and The Modular Nature Of The Tethermentioning

confidence: 99%

Integrase, LEDGF/p75 and HIV replication

Poeschla

2008

Cell. Mol. Life Sci.

115

104

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HIV integrates a DNA copy of its genome into a host cell chromosome in each replication cycle. The essential DNA cleaving and joining chemistry of integration is known, but there is less understanding of the process as it occurs in a cell, where two complex and dynamic macromolecular entities are joined: the viral pre-integration complex and chromatin. Among implicated cellular factors, much recent attention has coalesced around LEDGF/p75, a nuclear protein that may act as a chromatin docking factor or receptor for lentiviral pre-integration complexes. LEDGF/p75 tethers HIV integrase to chromatin, protects it from degradation, and strongly influences the genome-wide pattern of HIV integration. Depleting the protein from cells and/or over-expressing its integrase-binding domain blocks viral replication. Current goals are to establish the underlying mechanisms and to determine whether this knowledge can be exploited for antiviral therapy or for targeting lentiviral vector integration in human gene therapy.

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“…Each BRPF possesses a bromodomain and a proline-tryptophan-tryptophanproline-containing (PWWP) domain, with the former having the potential to recognize acetyl-lysine motifs (Seet et al, 2006). The PWWP domain is a 100-to 150-residue module with a highly conserved proline-tryptophan-tryptophan-proline motif and has been proposed to have methyl-lysine-binding ability (Stec et al, 2000;Maurer-Stroh et al, 2003).…”

Section: Moz and Morf As Catalytic Subunits Of Quartet Complexesmentioning

confidence: 99%

MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells

2007

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Genes of the human monocytic leukemia zinc-finger protein MOZ (HUGO symbol, MYST3) and its paralog MORF (MYST4) are rearranged in chromosome translocations associated with acute myeloid leukemia and/or benign uterine leiomyomata. Both proteins have intrinsic histone acetyltransferase activity and are components of quartet complexes with noncatalytic subunits containing the bromodomain, plant homeodomain-linked (PHD) finger and proline-tryptophan-tryptophan-proline (PWWP)-containing domain, three types of structural modules characteristic of chromatin regulators. Although leukemia-derived fusion proteins such as MOZ-TIF2 promote self-renewal of leukemic stem cells, recent studies indicate that murine MOZ and MORF are important for proper development of hematopoietic and neurogenic progenitors, respectively, thereby highlighting the importance of epigenetic integrity in safeguarding stem cell identity.

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The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation?

Cited by 203 publications

References 22 publications

Role of hepatoma‐derived growth factor in promoting de novo lipogenesis and tumorigenesis in hepatocellular carcinoma

Role of hepatoma‐derived growth factor in promoting de novo lipogenesis and tumorigenesis in hepatocellular carcinoma

Integrase, LEDGF/p75 and HIV replication

MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells

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