A short amino acid sequence able to specify nuclear location

Kalderon, Daniel; Roberts, Bruce; Richardson, William D.; Smith, Alan E.

doi:10.1016/0092-8674(84)90457-4

Cited by 2,397 publications

(1,714 citation statements)

References 24 publications

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“…This analysis recovered KR‐rich motifs that are part of the cNLS as the main motif of importin α cargos, and P‐rich motifs similar to the PY‐NLS as the main motif of transportin cargos (Lee et al , 2006), as expected (Table EV6), despite the limitation that DILIMOT is not designed to recover bipartite motifs. In both cases, the identified motifs are similar but not identical to the definitions proposed in previous literature (Kalderon et al , 1984; Dingwall et al , 1988; Lee et al , 2006), underlining that the respective signals exhibit a certain degree of plasticity. Surprisingly, this analysis also identified acidic stretches (DE‐rich motifs) to be significantly enriched in cargos of various importin β‐type NTRs but not, for example, transportins (Table EV6).…”

Section: Resultssupporting

confidence: 79%

Landscape of nuclear transport receptor cargo specificity

Mackmull

Klaus

Heinze

et al. 2017

Molecular Systems Biology

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Nuclear transport receptors (NTRs) recognize localization signals of cargos to facilitate their passage across the central channel of nuclear pore complexes (NPCs). About 30 different NTRs constitute different transport pathways in humans and bind to a multitude of different cargos. The exact cargo spectrum of the majority of NTRs, their specificity and even the extent to which active nucleocytoplasmic transport contributes to protein localization remains understudied because of the transient nature of these interactions and the wide dynamic range of cargo concentrations. To systematically map cargo–NTR relationships in situ, we used proximity ligation coupled to mass spectrometry (BioID). We systematically fused the engineered biotin ligase BirA* to 16 NTRs. We estimate that a considerable fraction of the human proteome is subject to active nuclear transport. We quantified the specificity and redundancy in NTR interactions and identified transport pathways for cargos. We extended the BioID method by the direct identification of biotinylation sites. This approach enabled us to identify interaction interfaces and to discriminate direct versus piggyback transport mechanisms. Data are available via ProteomeXchange with identifier PXD007976.

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Section: Resultssupporting

confidence: 79%

Landscape of nuclear transport receptor cargo specificity

Mackmull

Klaus

Heinze

et al. 2017

Molecular Systems Biology

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“…We have used this approach previously to demonstrate the role of CRM1 in the export of the predominantly nuclear protein BARD1 . As a positive control, we used Flag-Survivin þ NLS, a modified version of Survivin fused to the strong NLS of SV-40 large T antigen (Kalderon et al, 1984). As shown in Figure 3a (left panels), the SV-40 NLS-mediated import overcomes endogenous CRM1-dependent export of Survivin and enforces its steady-state localization in the nucleus when expressed alone.…”

Section: Resultsmentioning

confidence: 99%

Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown

et al. 2006

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As mitosis progresses, the chromosomal passenger proteins (CPPs) Survivin, Aurora B, INCENP and Borealin dynamically colocalize to mitotic structures. Chromosomal passenger proteins are already expressed during G2, whereas the nuclear envelope is only disassembled at the end of prophase. However, the mechanisms that modulate their nucleocytoplasmic localization before nuclear envelope breakdown (NEB) are poorly characterized. Using epitope-tagged proteins, we show that Aurora B, like Survivin, undergoes CRM1-mediated nucleocytoplasmic shuttling, although both proteins lack identifiable 'classical' nuclear transport signals. On the other hand, INCENP resides more stably in the nucleus and contains multiple nuclear localization signals. Finally, Borealin was detected in the nucleolus and the cytoplasm, but its cytoplasmic localization is not directly regulated by CRM1. Coexpression experiments indicate that the nuclear localization of Aurora B, but not of Survivin, is modulated by INCENP and that Survivin prevents the nucleolar accumulation of Borealin. Our data reveal that, in contrast to their closely related localization during mitosis, the nucleocytoplasmic localization of the CPPs before NEB is largely unrelated. Furthermore, the specific effect of INCENP and Survivin on the localization of Aurora B and Borealin, respectively, suggests that different complexes of CPPs may exist not only during mitosis, as recently reported, but also before NEB.

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“…Selective nuclear import occurs through the nuclear pore complex [39], which allows small molecules (under 45kDa) to diffuse freely into and out of the nucleus [39]. The targeting of larger proteins requires the presence of either a classical or a bipartite nuclear localization signal (NLS), both of which are composed of basic amino acids [40,41]. In this regard, a computational analysis of the entire amino acid sequence of each DAPC component showed that only the βdystroglycan contains a stretch of basic amino acids (RKKRKGK) that could correspond to an NLS (amino acids 776-782).…”

Section: Discussionmentioning

confidence: 99%

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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, et al.. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix.. Experimental Cell Research, Elsevier, 2006, 312 (16) ABSTRACT: Dystrophin is an essential component in the assembly and maintenance of the dystrophinassociated protein complex (DAPC), which includes members of the dystroglycan, syntrophin, sarcoglycan and dystrobrevin protein families. Distinctive complexes have been described in the cell membrane of different tissues and cultured cells. In this work, we report the identification and characterization of a novel DAPC present in the nuclei of HeLa cells, which contains dystrophin Dp71 as a key component. Using confocal microscopy and cell fractionation analyses, we found the presence of Dp71, β-sarcoglycan, β-dystroglycan, α-and β-syntrophin, α1-and β-dystrobrevin and nNOS in the nuclei of HeLa cells. Furthermore, we demonstrated by coimmunoprecipitation experiments that most of these proteins form a complex in the nuclear compartment. Next, we analyze the possible association of the nuclear DAPC with the nuclear matrix. We found the presence of Dp71, β-dystroglycan, nNOS, β-sarcoglycan, α/β syntrophin, α1-dystrobrevin and β-dystrobrevin in the nuclear matrix protein fractions and in situ nuclear matrix preparations from HeLa cells. Moreover, we found that Dp71, β-dystroglycan and β-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. The association of members of the nuclear DAPC with the nuclear matrix indicates that they may work as scaffolding proteins involved in nuclear architecture.

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A short amino acid sequence able to specify nuclear location

Cited by 2,397 publications

References 24 publications

Landscape of nuclear transport receptor cargo specificity

Landscape of nuclear transport receptor cargo specificity

Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

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