Transport across the nuclear envelope: Enigmas and explanations

Dingwall, Colin

doi:10.1002/bies.950130503

Cited by 61 publications

(30 citation statements)

References 42 publications

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“…We then determined cellular localization by immunohistochemistry. PHOX2B protein was localized to the nucleus in all assays except for the homeodomain deletion mutant, which also is missing a putative nuclear localization signal (Dingwall, 1991) (Figure 2b). …”

Section: Phox2b and Neuroblastomamentioning

confidence: 98%

Prevalence and functional consequence of PHOX2B mutations in neuroblastoma

et al. 2007

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Section: Phox2b and Neuroblastomamentioning

confidence: 98%

Prevalence and functional consequence of PHOX2B mutations in neuroblastoma

et al. 2007

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“…This provides a means for relaying signals originating from the plasma membrane to the nucleus while also offering the advantage of a rapid response time (7,22,24).…”

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confidence: 99%

Comparative analysis of the intracellular localization of c-Myc, c-Fos, and replicative proteins during cell cycle progression.

Vriz¹,

Lemaitre²,

Leibovici³

et al. 1992

Mol. Cell. Biol.

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In eukaryotic cells, nucleus-cytoplasm exchanges play an important role in genomic regulation. We have analyzed the localization of four nuclear antigens in different growth conditions: two replicative proteins, DNA polymerase a and proliferating cell nuclear antigen (PCNA), and two oncogenic regulatory proteins, c-Myc and c-Fos. A kinetic study of subcellular localization of these proteins has been done. In cultures in which cells were sparse, these proteins were detected in the nucleus. When proliferation was stopped by the high density of culture cells or by serum starvation, these proteins left the nucleus for the cytoplasm with different kinetics. DNA polymerase a is the first protein to leave the nucleus, with the PCNA protein, c-Fos, and c-Myc leaving the nucleus later. In contrast, during serum stimulation c-Fos and c-Myc relocalize into the nucleus before the replicative proteins. We also noticed that in sparse cell cultures, 10%/ of the cells exhibit a perinuclear staining for the DNA polymerase a, PCNA, and c-Myc proteins but not for c-Fos. This peculiar staining was also observed as an initial step to nuclear localization after serum stimulation and in vivo in Xenopus embryos when the G1 phase is reintroduced in the embryonic cell cycle at the mid-blastula stage. We suggest that such staining could reflect specific structures involved in the initiation of the S phase.In eukaryotic cells there is continuous exchange of macromolecules between the nucleoplasm and the cytoplasm, and one possible way to regulate the activity of a nuclear protein is to store it in the cytoplasm and control its access to the nucleus. This provides a means for relaying signals originating from the plasma membrane to the nucleus while also offering the advantage of a rapid response time (7,22,24).Nuclear localization is regulated for several proteins involved in gene expression and development, as well as for proteins involved in the cell cycle (see reference 12 for a review). For example, the activity of the dorsal morphogen is directly regulated by nuclear transport in selected regions of the Drosophila embryo (26,28,34). For the c-Fos protein, nuclear localization is dependent on continuous stimulation of cells by serum factors during cell growth, and in the absence of serum the protein is kept in the cytoplasm (27).In this study, the localization of four nuclear proteins which respond to the stimulation of cell growth was reanalyzed. c-myc and c-fos are two proto-oncogenes which are involved in regulatory events leading to the Gl-to-S transition and which are synthesized shortly after serum stimulation (see references 15, 17, and 25 for recent reviews). DNA polymerase a and proliferating cell nuclear antigen (PCNA), a subunit of DNA polymerase 8, are two proteins involved in the mechanism of eukaryotic DNA replication (see reference 39 for review). They are coordinately expressed with cell proliferation as a secondary event of serum stimulation (18,38). All four proteins have been found in the nuclei of growing cells in c...

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“…While small proteins (40-60 kD) often diffuse through the nuclear pore complex, nuclear entry of larger molecules and even of some small endogenous proteins, such as histones (Breeuwer and Goldfarb, 1990), is an active process mediated by specific nuclear localization signals (NLSs) contained in the transported molecule (Dingwall, 1991;GarciaBustos et al, 1991). That NLSs are relatively short, e.g.…”

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confidence: 99%

“…That NLSs are relatively short, e.g. 7 and 16 amino acid residues for the SV40 large T antigen NLS and Xenopus nucleoplasmin bipartite NLS, respectively (Smith et al, 1985;Goldfarb et al, 1986;Robbins et al, 1991), and often diverse in their amino acid composition (Dingwall, 1991;Garcia-Bustos et al, 1991) makes their identification difficult when based solely on amino acid sequence analysis. Moreover, even apparent consensus NLSs, such as the one present at the C terminus of the cytoplasmic protein GUS (Varagona et al, 1991;Citovsky et al, 1992), may not represent active signals.…”

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confidence: 99%

Yeast-Plant Coupled Vector System for Identification of Nuclear Proteins

Zaltsman

Yi²,

Krichevsky³

et al. 2007

Plant Physiology

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Nuclear proteins are involved in many critical biological processes within plant cells and, therefore, are in the focus of studies that usually begin with demonstrating that the protein of interest indeed exhibits nuclear localization. Thus, studies of plant nuclear proteins would be facilitated by a convenient experimental system for identification of proteins that are actively imported into the cell nucleus and visualization of their nuclear accumulation in vivo. To this end, we developed a system of vectors that allows screening for cDNAs coding for nuclear proteins in a simple genetic assay in yeast cells, and verification of nuclear accumulation in planta following one-step transfer and autofluorescent tagging of the identified clones into a multiple cloning site-compatible and reading frame-compatible plant expression vector. In a recommended third experimental step, the plant expression cassette containing the identified clone can be transferred, also by a one-step cloning, into a binary multigene expression vector for transient or stable coexpression with any other proteins.

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Transport across the nuclear envelope: Enigmas and explanations

Cited by 61 publications

References 42 publications

Prevalence and functional consequence of PHOX2B mutations in neuroblastoma

Prevalence and functional consequence of PHOX2B mutations in neuroblastoma

Comparative analysis of the intracellular localization of c-Myc, c-Fos, and replicative proteins during cell cycle progression.

Yeast-Plant Coupled Vector System for Identification of Nuclear Proteins

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