Major nucleolar proteins shuttle between nucleus and cytoplasm

Borer, R.A.; Lehner, Christian F.; Eppenberger, Hans M.; Nigg, Erich A.

doi:10.1016/0092-8674(89)90241-9

Cited by 1,054 publications

(773 citation statements)

References 68 publications

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“…Although specific nuclear export signals have been recently identified in a few proteins [27][28][29], there is also evidence arguing for nuclear export by a default pathway [30,31]. At present experimental evidence is lacking which could show whether Vigilin shuttles continuously across the nuclear envelope like some nucleolar proteins [32], the progesterone receptor [33] or some of the hnRNPs [27], or is stably anchored at the ER after it had passed by the nucleus.…”

Section: Vigilin Is Present Both In the Cytoplasm And In The Nucleusmentioning

confidence: 99%

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Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus

et al. 1996

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Vigilin is a member of the KH protein family and contains 14 tandemly arranged potential RNA-binding domains. Between KH domains 2 and 3 we have identified a nuclear localization sequence by cloning this sequence into the NH2-terminal region of phage T7 RNA polymerase as a reporter protein and by showing its transfer into the nucleus. Furthermore we provide experimental evidence that Vigilin is present both in the nucleus and in the cytoplasm in similar concentrations. These observations support the notion that Vigilin may shuttle between nucleus and cytoplasm presumably in contact with RNA molecules.

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Section: Vigilin Is Present Both In the Cytoplasm And In The Nucleusmentioning

confidence: 99%

“…This observation renders Vigilin different from other proteins shuttling between the cytoplasm and the nucleus, which are predominantly nuclear at equilibrium conditions [27,32].…”

Section: Vigilin Does Not Accumulate Either In the Nucleus Or In Thementioning

confidence: 99%

Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus

et al. 1996

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“…Preliminary studies by Finlay and Forbes [19901 suggest the presence of 8-10 different possible NLSreceptor molecules associated with the nuclear pore. NLS-binding polypeptides, shuttling between the cytoplasm and the nucleoplasm or the nucleolus, may be present in addition to those associated with the pore [Borer et al, 1989;Yamasaki et al, 1989;Adam et al, 1989;Blobel, 1990, 1992;Lee et al, 1991;Li et al, 19921.…”

Section: Nls-binding Proteinsmentioning

confidence: 99%

Putative nuclear localization signals (NLS) in protein transcription factors

Boulikas

1994

J of Cellular Biochemistry

188

121

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We have recognized about ten distinct forms of strongly basic hexapeptides, containing at least four arginines and lysines, characteristic of nuclear proteins among all eukaryotic species, including yeast, plants, flies and mammals. These basic hexapeptides are considered to be different versions of a core nuclear localization signal, NLS. Core NLSs are present in nearly all nuclear proteins and absent from nearly all "nonassociated" cytoplasmic proteins that have been investigated. We suggest that the few ( -10%) protein factors lacking a typical NLS core peptide may enter the nucleus via their strong crosscomplexation with their protein factor partners that possess a core NLS. Those cytoplasmic proteins found to possess a NLS-like peptide are either tightly associated with cell membrane proteins or are integral components of large cytoplasmic protein complexes. On the other hand, some versions of core NLSs are found in many cell membrane proteins and secreted proteins. It is hypothesized that in these cases the N-terminal hydrophobic signal peptide of extracellular proteins and the internal hydrophobic domains of transmembrane proteins are stronger determinants for their subcellular localization. The position of core NLSs among homologous nuclear proteins may or may not be conserved; however, if lost from an homolgous site it appears elsewhere in the protein.This search provides a set of rules to our understanding of the nature of core nuclear localization signals: (1 ) Core NLS are proposed to consist most frequently of an hexapeptide with 4 arginines and lysines; ( 2 ) aspartic and glutamic acid residues as well as bulky amino acids (F, Y, W) need not to be present in this hexapeptide; (3) acidic residues and proline or glycine that break the a-helix are frequently in the flanking region of this hexapeptide stretch; (4) hydrophobic residues ought not to be present in the core NLS flanking region allowing for the NLS to be exposed on the protein. In this study we attempt to classify putative core NLS from a wealth of nuclear protein transcription factors from diverse species into several categories, and we propose additional core NLS structures yet to be experimentally verified. Key words: pore complex, transporter proteins, transcription factors, nuclear localization, nuclear proteins, basic region, cytoplasmic proteins, membrane proteins, c-Myc, c-Jun, NF-KB The nuclear envelope effectively separates transcription of genes from translation of their mRNA into proteins and allows proteins destined to function in the nucleus to pass selectively through the lumen of the nuclear pores [reviewed by Newport and Forbes, 1987; Boulikas, 19871. Pore complexes are anchored to the double nuclear membrane via the transmembrane glycoprotein gp210 [Wozniak et al., 19891 and with the aqueous channel that has an effective diameter of approximately 10 nm allow small proteins with a molecular weight inferior ~~ Abbreviations: ER, endoplasmic reticulum; aa, amino acid(s); NLS, nuclear localization signal.

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“…NPM is a highly conserved nonribosomal RNAbinding nucleolar phosphoprotein, one of which function is a shuttle protein, transporting ribosomal ribonucleoproteins (rRNPs) between the nucleolus and the cytoplasm during the assembly of ribosomes (Schmidt-Zachmann et al, 1987;Borer et al, 1989). NPM forms a hexameric homo-oligomer (assembled in a head-to-head/tail-to-tail fashion) as it shuttles between subcellular compartments (Yung and Chan, 1987;Schmidt-Zachmann and Franke, 1988;Liu and Chan, 1991).…”

Section: Introductionmentioning

confidence: 99%

Apoptosis induced by the myelodysplastic syndrome-associated NPM-MLF1 chimeric protein

1999

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The NPM-MLF1 chimeric protein is produced by the t(3;5)(q25.1;q34) chromosomal translocation, which is associated with myelodysplastic syndrome (MDS) prior to progression into acute myeloid leukemia (AML). Here we report that K562 human leukemia cells ectopically expressing NPM-MLF1, but not those with wild-type MLF1, were gradually eliminated from the culture by undergoing apoptosis. NIH3T3 mouse ®broblasts engineered to overexpress NPM-MLF1 grew normally but serum deprivation triggered apoptotic cell death with slower kinetics than did other well-known apoptotic inducers such as c-Myc or E2F-1. Quantitative analysis of apoptotic induction con®rmed that, neither NPM nor MLF1, but the NPM-MLF1 fusion protein was able to induce apoptosis. Analyses using a variety of deletion mutants of NPM-MLF1 revealed that induction of apoptosis required the N-terminal domain of MLF1 and the NPM domain containing nuclear localization signal and that removal of the NPM dimerization domain markedly impaired the ability to induce apoptosis. Co-expression of Bcl-2 rescued NIH3T3 ®broblasts from NPM-MLF1-mediated cell death without a ecting the expression level or the subcellular localization of NPM-MLF1 and enabled cells to progress into S phase in low serum. These ®ndings provide an NPM-MLF1-mediated novel mechanism of apoptotic induction and imply that NPM-MLF1 in collaboration with anti-apoptotic oncoproteins may play an important role in multi-step progression from MDS to AML.

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Major nucleolar proteins shuttle between nucleus and cytoplasm

Cited by 1,054 publications

References 68 publications

Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus

Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus

Putative nuclear localization signals (NLS) in protein transcription factors

Apoptosis induced by the myelodysplastic syndrome-associated NPM-MLF1 chimeric protein

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