| Knockout of AMD-associated gene POLDIP2 reduces mitochondrial superoxide in human retinal pigment epithelial cells. | Knockout of AMD-associated gene POLDIP2 reduces mitochondrial superoxide in human retinal pigment epithelial cells.
Nguyen T, Urrutia-Cabrera D, Wang L, Lees JG, Wang JH, Hung SSC, Hewitt AW, Edwards TL, McLenachan S, Chen FK, Lim SY, Luu CD, Guymer R, Wong RCB., Free PMC Article | 10/23/2023 |
| Metabolic regulation of the proteasome under hypoxia by Poldip2 controls fibrotic signaling in vascular smooth muscle cells. | Metabolic regulation of the proteasome under hypoxia by Poldip2 controls fibrotic signaling in vascular smooth muscle cells.
Paredes F, Williams HC, Suster I, Tejos M, Fuentealba R, Bogan B, Holden CM, San Martin A., Free PMC Article | 01/21/2023 |
| Endothelial Poldip2 regulates sepsis-induced lung injury via Rho pathway activation. | Endothelial Poldip2 regulates sepsis-induced lung injury via Rho pathway activation.
Dolmatova EV, Forrester SJ, Wang K, Ou Z, Williams HC, Joseph G, Kumar S, Valdivia A, Kowalczyk AP, Qu H, Jo H, Lassègue B, Hernandes MS, Griendling KK., Free PMC Article | 09/3/2022 |
| Poldip2/Nox4 Mediates Lipopolysaccharide-Induced Oxidative Stress and Inflammation in Human Lung Epithelial Cells. | Poldip2/Nox4 Mediates Lipopolysaccharide-Induced Oxidative Stress and Inflammation in Human Lung Epithelial Cells.
Wang Y, Ding Z, Tu Y, Wu X, Zhang W, Ji S, Shen J, Zhang L, Wu H, Fei G., Free PMC Article | 04/2/2022 |
| Crystal structure and molecular dynamics of human POLDIP2, a multifaceted adaptor protein in metabolism and genome stability. | Crystal structure and molecular dynamics of human POLDIP2, a multifaceted adaptor protein in metabolism and genome stability.
Kulik AA, Maruszczak KK, Thomas DC, Nabi-Aldridge NLA, Carr M, Bingham RJ, Cooper CDO., Free PMC Article | 12/25/2021 |
| MIR31HG regulates the proliferation, migration and invasion of breast cancer by regulating the expression of POLDIP2. | MIR31HG regulates the proliferation, migration and invasion of breast cancer by regulating the expression of POLDIP2.
Xin C, Bi X, Xiao C, Dong L. | 12/18/2021 |
| [PolDIP2 regulates mitochondrial functioning and cellular metabolism].", trans "PolDIP2, une proteine cle de la regulation du fonctionnement mitochondrial et du metabolisme cellulaire. | [PolDIP2 regulates mitochondrial functioning and cellular metabolism].
Andjongo É, Benhamouche S, Bouraoui A, Baciou L. | 10/30/2021 |
| Human Polymerase delta-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils. | Human Polymerase δ-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils.
Kasho K, Krasauskas L, Smirnovas V, Stojkovič G, Morozova-Roche LA, Wanrooij S., Free PMC Article | 07/3/2021 |
| Poldip2 deficiency in human aortic vascular smooth muscle in vitro induces the expression of the SRF , myocardin, and MRTFA and dramatically represses KLF4. Poldip2 deficiency upregulates the hexosamine biosynthetic pathway and OGT (O-linked N-acetylglucosamine transferase)-mediated protein O-GlcNAcylation. Poldip2 deficiency induces a highly differentiated phenotype in VSMCs by regulating metabolism and proteostasis. | Mitochondrial Protein Poldip2 (Polymerase Delta Interacting Protein 2) Controls Vascular Smooth Muscle Differentiated Phenotype by O-Linked GlcNAc (N-Acetylglucosamine) Transferase-Dependent Inhibition of a Ubiquitin Proteasome System.
Paredes F, Williams HC, Quintana RA, San Martin A., Free PMC Article | 08/1/2020 |
| functional interaction of PolDIP2 with human DNA polymerases and the possible functions in DNA damage response | A Multifunctional Protein PolDIP2 in DNA Translesion Synthesis.
Gagarinskaya DI, Makarova AV. | 07/25/2020 |
| Poldip2 and Ect2 are both essential for vascular smooth muscle cell cytokinesis and proliferation. | Polymerase-δ-interacting protein 2 activates the RhoGEF epithelial cell transforming sequence 2 in vascular smooth muscle cells.
Huff LP, Kikuchi DS, Faidley E, Forrester SJ, Tsai MZ, Lassègue B, Griendling KK., Free PMC Article | 02/15/2020 |
| The loss of PDIP38 consistently causes a shift in DNA damage tolerance (DDT) from error-prone translesion DNA synthesis (TLS) to error-free template switching (TS) without enhancing cellular sensitivity to DNA damage. We propose that PDIP38 controls the relative usage of TLS and TS increasing usage of TLS without changing the overall capability of DDT. | PDIP38/PolDIP2 controls the DNA damage tolerance pathways by increasing the relative usage of translesion DNA synthesis over template switching.
Tsuda M, Ogawa S, Ooka M, Kobayashi K, Hirota K, Wakasugi M, Matsunaga T, Sakuma T, Yamamoto T, Chikuma S, Sasanuma H, Debatisse M, Doherty AJ, Fuchs RP, Takeda S., Free PMC Article | 12/7/2019 |
| Integrin engagement during cell attachment activates Poldip2/Nox4 to oxidize actin, which modulates filamentous actin assembly and its interaction with vinculin. | NOX4 (NADPH Oxidase 4) and Poldip2 (Polymerase δ-Interacting Protein 2) Induce Filamentous Actin Oxidation and Promote Its Interaction With Vinculin During Integrin-Mediated Cell Adhesion.
Vukelic S, Xu Q, Seidel-Rogol B, Faidley EA, Dikalova AE, Hilenski LL, Jorde U, Poole LB, Lassègue B, Zhang G, Griendling KK., Free PMC Article | 08/10/2019 |
| that demonstrated that POLDIP2 gene was function as an oncogene in NSCLC and implied the oncogenic ability might be through promoting cell proliferation or Epithelial-mesenchymal transition | Knockdown of POLDIP2 suppresses tumor growth and invasion capacity and is linked to unfavorable transformation ability and metastatic feature in non-small cell lung cancer.
Chen YC, Kuo CC, Chian CF, Tzao C, Chang SY, Shih YL, Lin YW, Yu MH, Su HY. | 04/6/2019 |
| Increasing mitochondrial lipoylation by forced expression of Poldip2 increases respiration and reduces the growth rate of cancer cells. Study unveils a regulatory mechanism of catabolic enzymes required for metabolic plasticity and highlights the role of Poldip2 as key during hypoxia and cancer cell metabolic adaptation. | Poldip2 is an oxygen-sensitive protein that controls PDH and αKGDH lipoylation and activation to support metabolic adaptation in hypoxia and cancer.
Paredes F, Sheldon K, Lassègue B, Williams HC, Faidley EA, Benavides GA, Torres G, Sanhueza-Olivares F, Yeligar SM, Griendling KK, Darley-Usmar V, San Martin A., Free PMC Article | 08/18/2018 |
| findings establish that PolDIP2 can regulate the translesion synthesis polymerase and primer extension activities of PrimPol | PolDIP2 interacts with human PrimPol and enhances its DNA polymerase activities.
Guilliam TA, Bailey LJ, Brissett NC, Doherty AJ., Free PMC Article | 09/24/2016 |
| POLDIP2 plays a crucial role in Tau aggregation via the impairment of autophagy activity, providing insight into Tau aggregation in Tau pathology. | Essential role of POLDIP2 in Tau aggregation and neurotoxicity via autophagy/proteasome inhibition.
Kim Y, Park H, Nah J, Moon S, Lee W, Hong SH, Kam TI, Jung YK. | 08/8/2015 |
| PDIP38 can respond to genotoxic or transcriptional stresses by undergoing translocation to the spliceosomes, where it is a required participant in the regulation of MDM2 alternative splicing. | 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 A, Zhang S, Mordue D, Wu JM, Zhang Z, Darzynkiewicz Z, Lee EY, Lee MY., Free PMC Article | 04/19/2014 |
| DNA polymerase delta-interacting protein 2 is a processivity factor for DNA polymerase lambda during 8-oxo-7,8-dihydroguanine bypass. | DNA polymerase δ-interacting protein 2 is a processivity factor for DNA polymerase λ during 8-oxo-7,8-dihydroguanine bypass.
Maga G, Crespan E, Markkanen E, Imhof R, Furrer A, Villani G, Hübscher U, van Loon B., Free PMC Article | 01/25/2014 |
| We demonstrate that PDIP38 (Poldelta interacting protein of 38kDa) directly interacts with the TLS polymerase Poleta. PDIP38 is able to interact directly not only with Poleta but also with the specialized polymerases Rev1 and Polzeta (via Rev7). | Crosstalk between replicative and translesional DNA polymerases: PDIP38 interacts directly with Poleta.
Tissier A, Janel-Bintz R, Coulon S, Klaile E, Kannouche P, Fuchs RP, Cordonnier AM. | 01/8/2011 |
| Observational study of gene-disease association. (HuGE Navigator) | Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article | 12/5/2010 |
| suggest that the TNFAIP1/POLDIP2 complex sense-antisense architecture represents a clinically significant transcriptional structural-functional gene module associated with amplification of the genomic region on 17q11.2 in breast cancer. | Complex sense-antisense architecture of TNFAIP1/POLDIP2 on 17q11.2 represents a novel transcriptional structural-functional gene module involved in breast cancer progression.
Grinchuk OV, Motakis E, Kuznetsov VA., Free PMC Article | 04/12/2010 |
| Poldip2 associates with p22phox to activate Nox4, leading to regulation of focal adhesion turnover and vascular smooth muscle cell migration, thus linking reactive oxygen species production and cytoskeletal remodeling. | Poldip2, a novel regulator of Nox4 and cytoskeletal integrity in vascular smooth muscle cells.
Lyle AN, Deshpande NN, Taniyama Y, Seidel-Rogol B, Pounkova L, Du P, Papaharalambus C, Lassègue B, Griendling KK., Free PMC Article | 01/21/2010 |
| PDIP38 is located in the mitochondrial matrix. TFAM and mitochondrial single-stranded DNA binding protein (mtSSB) are co-immunoprecipitated with PDIP38 | PDIP38 associates with proteins constituting the mitochondrial DNA nucleoid.
Cheng X, Kanki T, Fukuoh A, Ohgaki K, Takeya R, Aoki Y, Hamasaki N, Kang D. | 01/21/2010 |
| PDIP38 can shuttle between the cytoplasmic and the nuclear compartments and that its subcellular localization is regulated by CEACAM1 | The cell adhesion receptor carcinoembryonic antigen-related cell adhesion molecule 1 regulates nucleocytoplasmic trafficking of DNA polymerase delta-interacting protein 38.
Klaile E, Müller MM, Kannicht C, Otto W, Singer BB, Reutter W, Obrink B, Lucka L. | 01/21/2010 |