PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2

Wong, Agnes; Zhang, Sufang; Mordue, Dana G.; Wu, Joseph M.; Zhang, Zhongtao; Darzynkiewicz, Zbigniew; Lee, Ernest Y.C.; Lee, Marietta Y.W.T.

doi:10.4161/cc.26221

Cited by 30 publications

(36 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Using the technique of UV exposure through UV-opaque polycarbonate filters with 5 or 10 μm pores to create local areas of irradiation [84], it was observed that PDIP38 was not recruited to these DNA damage foci, in contrast to Pol η and PCNA [199]. This finding does not negate the proposal that PDIP38 is involved in Pol η recruitment [190], since the mechanism is unknown and might involve a transient association of PDIP38 to DNA damage sites.…”

Section: Pdip38 Responds To Genotoxic and Transcriptional Stress By Tcontrasting

confidence: 42%

“…Thus, the translocation of PDIP38 to the spliceosomes is a novel DNA damage response [199]. In addition to genotoxic stress, transcriptional stress induced by α-amanitin also led to translocation of PDIP38 to the nuclear speckles [199]. Interestingly, the human DNA glycosylase hOGG1 is also translocated to the nuclear speckles under the influence of UVA [201].…”

Section: Pdip38 Responds To Genotoxic and Transcriptional Stress By Tmentioning

confidence: 99%

See 1 more Smart Citation

Regulation and Modulation of Human DNA Polymerase δ Activity and Function

Lee

Wang

Zhang

et al. 2017

Preprint

Self Cite

View full text Add to dashboard Cite

This review focuses on the regulation and modulation of human DNA polymerase δ (Pol δ). The emphasis is on mechanisms that regulate the activity and properties of Pol δ in DNA repair and replication. The areas covered are the degradation of the p12 subunit of Pol δ, which converts it from a heterotetramer (Pol δ4) to a heterotrimer (Pol δ3), in response to DNA damage and also during the cell cycle. The biochemical mechanisms that lead to degradation of p12 are reviewed, as well as the properties of Pol δ4 and Pol δ3 that provide insights into their functions in DNA replication and repair. The second focus of the review involves the functions of two Pol δ binding proteins, PDIP46 and PDIP38, both of which are multi-functional proteins. PDIP46 is a novel activator of Pol δ4, and the impact of this function is discussed in relation to its potential roles in DNA replication. Several new models for the roles of Pol δ3 and Pol δ4 in leading and lagging strand DNA synthesis that integrate a role for PDIP46 are presented. PDIP38 has multiple cellular localizations including the mitochondria, the splicesosomes and the nucleus. It has been implicated in a number of cellular functions, including the regulation of specialized DNA polymerases, mitosis, the DNA damage response, Mdm2 alternative splicing and the regulation of the Nox4 NADPH oxidase.

show abstract

Section: Pdip38 Responds To Genotoxic and Transcriptional Stress By Tcontrasting

confidence: 42%

Section: Pdip38 Responds To Genotoxic and Transcriptional Stress By Tmentioning

confidence: 99%

Regulation and Modulation of Human DNA Polymerase δ Activity and Function

Lee

Wang

Zhang

et al. 2017

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…Poldip2 is fairly ubiquitously expressed, having been reported in aorta, 3, 4 lung, 3 kidney, 3, 5, 6 heart 7 and thyroid, 8 as well as many cell types including mouse aortic smooth muscle cells, 9 astrocytes, 10 vascular smooth muscle cells (VSMC), 3, 11 brain endothelial cells, 12 epithelial cells, 12 HeLa, 1, 12-15 fibroblasts, 2, 13, 16, 17 kidney fibroblasts, 18 myoblasts, 19 human umbilical vein endothelial cells, 20 human embryonic kidney cells 293 (HEK 293), 13 MRC5 cells, 21, 22 and cortical neurons. 23 There is also evidence of Poldip2 expression in human breast cancer, 24 human breast adenocarcinoma cells 13 and human lung adenocarcinoma cells.…”

Section: Tissue Expressionmentioning

confidence: 99%

Polymerase δ-interacting Protein 2: A Multifunctional Protein

Hernandes

Lassègue

Griendling

2017

Journal of Cardiovascular Pharmacology

View full text Add to dashboard Cite

Polymerase δ-interacting protein 2 (Poldip2) is a multi-functional protein originally described as a binding partner of the p50 subunit of DNA polymerase δ and proliferating cell nuclear antigen. In addition to its role in DNA replication and damage repair, Poldip2 has been implicated in mitochondrial function, extracellular matrix regulation, cell cycle progression, focal adhesion turnover and cell migration. However, Poldip2 functions are incompletely understood. In this review, we discuss recent literature on Poldip2 tissue distribution, subcellular localization, and function. We also address the putative function of Poldip2 in cardiovascular disease, neurodegenerative conditions and in renal pathophysiology.

show abstract

“…Thus, Poldip2 is necessary for vascular integrity and function. 17 However, in addition to regulating Nox4, Poldip2 has a number of other reported functions, including roles in organizing the mitotic spindle, DNA repair, and cellular adhesion 18 19-21 . Many of these processes can potentially contribute to collateralogenesis.…”

Section: Introductionmentioning

confidence: 99%

Polymerase δ-Interacting Protein 2 Promotes Postischemic Neovascularization of the Mouse Hindlimb

Amanso

Lassègue

Joseph

et al. 2014

ATVB

View full text Add to dashboard Cite

Objective Collateral vessel formation can functionally compensate for obstructive vascular lesions in patients with atherosclerosis. Neovascularization processes are triggered by fluid shear stress, hypoxia, growth factors, chemokines, proteases and inflammation, as well as reactive oxygen species (ROS) in response to ischemia. Poldip2 is a multifunctional protein that regulates focal adhesion turnover and vascular smooth muscle cell migration and modifies extracellular matrix composition. We therefore tested the hypothesis that loss of Poldip2 impairs collateral formation. Approach and Results The mouse hindlimb ischemia model has been used to understand mechanisms involved in postnatal blood vessel formation. Poldip2+/- mice were subjected to femoral artery excision, and functional and morphological analysis of blood vessel formation was performed after injury. Heterozygous deletion of Poldip2 decreased the blood flow recovery and spontaneous running activity at 21 days after injury. H2O2 production, as well as the activity of matrix metalloproteinases-2 and -9, was reduced in these animals compared with Poldip2+/+ mice. Infiltration of macrophages in the peri-injury muscle was also decreased; however, macrophage phenotype was similar between genotypes. In addition, the formation of capillaries and arterioles was impaired, as was angiogenesis, in agreement with a decrease in proliferation observed in endothelial cells treated with siRNA against Poldip2. Finally, regression of newly formed vessels and apoptosis was more pronounced in Poldip2+/- mice. Conclusions Together, these results suggest that Poldip2 promotes ischemia-induced collateral vessel formation via multiple mechanisms that likely involve ROS-dependent activation of matrix metalloproteinase activity as well as enhanced vascular cell growth and survival.

show abstract

PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2

Abstract: (2013) PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UVinduced alternative splicing of MDM2, Cell Cycle, 12:19,[3373][3374][3375][3376][3377][3378][3379][3380][3381][3382]

Cited by 30 publications

References 59 publications

Regulation and Modulation of Human DNA Polymerase δ Activity and Function

Regulation and Modulation of Human DNA Polymerase δ Activity and Function

Polymerase δ-interacting Protein 2: A Multifunctional Protein

Polymerase δ-Interacting Protein 2 Promotes Postischemic Neovascularization of the Mouse Hindlimb

Contact Info

Product

Resources

About

PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2

Abstract: (2013) PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UVinduced alternative splicing of MDM2, Cell Cycle, 12:19,[3373][3374][3375][3376][3377][3378][3379][3380][3381][3382]

Cited by 30 publications

References 59 publications

Regulation and Modulation of Human DNA Polymerase &delta; Activity and Function

Regulation and Modulation of Human DNA Polymerase &delta; Activity and Function

Polymerase δ-interacting Protein 2: A Multifunctional Protein

Polymerase δ-Interacting Protein 2 Promotes Postischemic Neovascularization of the Mouse Hindlimb

Contact Info

Product

Resources

About

Regulation and Modulation of Human DNA Polymerase δ Activity and Function

Regulation and Modulation of Human DNA Polymerase δ Activity and Function