ArticleMolecular and cellular biology2002
RGS12TS-S localizes at nuclear matrix-associated subnuclear structures and represses transcription: structural requirements for subnuclear targeting and transcriptional repression.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Distinct and overlapping RGS14 and RGS12 actions regulate NPT2A-mediated phosphate transport.Biochemical and biophysical research communications · 2024Article
- Rgs1 is a regulator of effector gene expression during plant infection by the rice blast fungusProceedings of the National Academy of Sciences of the United States of America · 2023Article
- RGS12 is a novel tumor suppressor in osteosarcoma that inhibits YAP-TEAD1-Ezrin signaling.Oncogene · 2021Article
- RGS12 is required for the maintenance of mitochondrial function during skeletal development.Cell discovery · 2020Article
- A role for Regulator of G protein Signaling-12 (RGS12) in the balance between myoblast proliferation and differentiation.PloS one · 2019Article
- 14-3-3γ binds regulator of G protein signaling 14 (RGS14) at distinct sites to inhibit the RGS14:GαThe Journal of biological chemistry · 2018Article
- Genetic Analysis of Rare Human Variants of Regulators of G Protein Signaling Proteins and Their Role in Human Physiology and Disease.Pharmacological reviews · 2018Review
- Article
- RGS17: an emerging therapeutic target for lung and prostate cancers.Future medicinal chemistry · 2013Article
- Non-canonical functions of RGS proteins.Cellular signalling · 2010Review
- RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways.Cellular signalling · 2010Article
- Regulation of Smad-mediated gene transcription by RGS3.Molecular pharmacology · 2008Article
- Identification of a common subnuclear localization signal.Molecular biology of the cell · 2007Article
- Towards understanding the epigenetics of transcription by chromatin structure and the nuclear matrix.Gene therapy & molecular biology · 2005Article
- Psychostimulants, madness, memory... and RGS proteins?Neuromolecular medicine · 2005Review
- Pka, Ras and RGS protein interactions regulate activity of AflR, a Zn(II)2Cys6 transcription factor in Aspergillus nidulans.Genetics · 2003Article
- Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140.Molecular and cellular biology · 2003Article
- Human genetic variants disrupt RGS14 nuclear shuttling and regulation of LTP in hippocampal neurons.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
RGS12TS-S, an 1,157-amino-acid RGS protein (regulator of G protein signaling), is a nuclear protein that exhibits a unique pattern of subnuclear organization into nuclear foci or dots when expressed endogenously or ectopically. We now report that RGS12TS-S is a nuclear matrix protein and identify structural determinants that target this protein to the nuclear matrix and to discrete subnuclear sites. We also determine the relationship between RGS12TS-S-decorated nuclear dots and known subnuclear domains involved in control of gene expression and provide the first evidence that RGS12TS-S is functionally involved in the regulation of transcription and cell cycle events. A novel nuclear matrix-targeting sequence was identified that is distinct from a second novel motif needed for targeting RGS12TS-S to nuclear dots. RGS12TS-S nuclear dots were distinct from Cajal bodies, SC-35 domains, promyelocytic leukemia protein nuclear bodies, Polycomb group domains, and DNA replication sites. However, RGS12TS-S inhibited S-phase DNA synthesis in various tumor cell lines independently of Rb and p53 proteins, and its prolonged expression promoted formation of multinucleated cells. Expression of RGS12TS-S dramatically reduced bromo-UTP incorporation into sites of transcription. RGS12TS-S, when tethered to a Gal4 DNA binding domain, dramatically inhibited basal transcription from a Gal4-E1b TATA promoter in a histone deacetylase-independent manner. Structural analysis revealed a role for the unique N-terminal domain of RGS12TS-S in its transcriptional repressor and cell cycle-regulating activities and showed that the RGS domain was dispensable for these functions. These results provide novel insights into the structure and function of RGS12TS-S in the nucleus and demonstrate that RGS12TS-S possesses biological activities distinct from those of other members of the RGS protein family.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.