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.
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.
Integrin engagement during cell attachment activates Poldip2/Nox4 to oxidize actin which modulates filamentous actin assembly and its interaction with vinculin.
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
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.
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.
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).
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.
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.
PDIP38 is located in the mitochondrial matrix. TFAM and mitochondrial single-stranded DNA binding protein (mtSSB) are co-immunoprecipitated with PDIP38
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