ArticleThe Biochemical journal1995
Protein 4.1 is a component of the nuclear matrix of mammalian cells.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 76 citations in OpenAlex.
- FERM domain-containing proteins are active components of the cell nucleus.Life science alliance · 2024Review
- Cytoskeletal Protein 4.1R in Health and Diseases.Biomolecules · 2024Review
- Caveolin-1α regulates primary cilium length by controlling RhoA GTPase activity.Scientific reports · 2019Article
- Alternative polyadenylation in a family of paralogous EPB41 genes generates protein 4.1 diversity.RNA biology · 2017Article
- Impaired intestinal calcium absorption in protein 4.1R-deficient mice due to altered expression of plasma membrane calcium ATPase 1b (PMCA1b).The Journal of biological chemistry · 2013Article
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Journal of cell science · 2011Article
- Rolly protein (ROLP)-Epb4.1/3: a potential protein-protein interaction relevant for the maintenance of cell adhesion.International journal of molecular sciences · 2009Article
- Inhibition of protein 4.1 R and NuMA interaction by mutagenization of their binding-sites abrogates nuclear localization of 4.1 R.Clinical and translational science · 2009Article
- An internal ribosome entry site element directs the synthesis of the 80 kDa isoforms of protein 4.1R.BMC biology · 2008Article
- Downregulation of protein 4.1R, a mature centriole protein, disrupts centrosomes, alters cell cycle progression, and perturbs mitotic spindles and anaphase.Molecular and cellular biology · 2008Article
- Protein 4.1R self-association: identification of the binding domain.The Biochemical journal · 2006Article
- Cell cycle-dependent nucleocytoplasmic shuttling of the neurofibromatosis 2 tumour suppressor merlin.Oncogene · 2005Article
- Towards understanding the epigenetics of transcription by chromatin structure and the nuclear matrix.Gene therapy & molecular biology · 2005Article
- Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase.Molecular biology of the cell · 2005Article
- Identification of a novel microtubule-destabilizing motif in CPAP that binds to tubulin heterodimers and inhibits microtubule assembly.Molecular biology of the cell · 2004Article
- Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- A nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibers.Molecular biology of the cell · 2000Article
- The N-terminal 209-aa domain of high molecular-weight 4.1R isoforms abrogates 4.1R targeting to the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R.Molecular biology of the cell · 1999Article
- A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein.The Journal of cell biology · 1999Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein 4.1 is a major component of the erythrocyte membrane skeleton that promotes the interaction of spectrin with actin and links the resulting complex network to integral membrane proteins. Here we analyse the distribution of different 4.1 proteins within the nucleus of mammalian cells. Nuclear matrices have been prepared from Madin-Darby canine kidney (MDCK) and HeLa cells and protein fractions isolated at each step of the purifications have been analysed by immunoblotting using characterized polyclonal antibodies against protein 4.1. Two 4.1 polypeptides of M(r) approximately 135,000 and 175,000 are extracted after DNase I digestion and 0.25 M ammonium sulphate treatments, suggesting that they may be associated with chromatin. Interestingly, nuclear matrices isolated after DNase I digestion and sequential treatments with increasing ionic strength contain a third 4.1 polypeptide of M(r) approximately 75,000 (4.1p75), suggesting that it is a component of the nuclear matrix. Immunoblot analyses of nuclear matrices isolated from different cell types and species indicate that 4.1p75 is a common element of the nuclear matrix of mammalian cells. Moreover, 4.1p75 distributes to typical nuclear speckles which are enriched with the spliceosome assembly factor SC35, as revealed by double-label immunofluorescence analyses. Protein 4.1p75 might be an anchoring element of the nucleoskeleton, playing a role similar to that described for the erythroid protein 4.1 in red blood cells.
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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.