ArticleMolecular and cellular biology2005
Sumoylation of the novel protein hRIP{beta} is involved in replication protein A deposition in PML nuclear bodies.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- On the Prevalence and Roles of Proteins Undergoing Liquid-Liquid Phase Separation in the Biogenesis of PML-Bodies.Biomolecules · 2023Article
- Rtt105 promotes high-fidelity DNA replication and repair by regulating the single-stranded DNA-binding factor RPA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Association of the host genetic factors, hypercholesterolemia and diabetes with mild influenza in an Iranian population.Virology journal · 2021Article
- PRMT5 inhibition disrupts splicing and stemness in glioblastoma.Nature communications · 2021Article
- PML-mediated signaling and its role in cancer stem cells.Oncogene · 2014Review
- Promyelocytic leukemia protein is a cell-intrinsic factor inhibiting parvovirus DNA replication.Journal of virology · 2014Article
- Replication protein A safeguards genome integrity by controlling NER incision events.The Journal of cell biology · 2011Article
- Elevated level of SUMOylated IRF-1 in tumor cells interferes with IRF-1-mediated apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment.Molecular and cellular biology · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replication protein A (RPA) is a single-stranded-DNA-binding protein composed of three subunits with molecular masses of 70, 32, and 14 kDa. The protein is involved in multiple processes of eukaryotic DNA metabolism, including DNA replication, repair, and recombination. In Xenopus, Xenopus RPA-interacting protein alpha has been identified as a carrier molecule of RPA into the nucleus. In this study, human RPA-interacting protein alpha (hRIPalpha) and five novel splice isoforms (named hRIPalpha, hRIPbeta, hRIPgamma, hRIPdelta1, hRIPdelta2, and hRIPdelta3 according to the lengths of their encoding peptides) were cloned. Among hRIP isoforms, hRIPalpha and hRIPbeta were found to be the major splice isoforms and to show different subcellular localizations. While hRIPalpha localized to the cytoplasm, hRIPbeta was found in the PML nuclear body. Modification of hRIPbeta by sumoylation was found to be required for localization to the PML nuclear body. The results of the present work demonstrate that hRIPbeta transports RPA into the PML nuclear body and releases RPA upon UV irradiation. hRIPbeta thus plays an important role in RPA deposition in PML nuclear bodies and thereby supplements RPA for DNA metabolism.
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