Evidence map›Paper›PMID 22847741›Full record

ArticleCell research2012

Chromatin-bound NLS proteins recruit membrane vesicles and nucleoporins for nuclear envelope assembly via importin-α/β.

Quanlong Lu, Zhigang Lu, Qinying Liu, Li Guo, He Ren, Jingyan Fu, Qing Jiang, Paul R Clarke, Chuanmao Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 20 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Quanlong LuState Key Laboratory of Bio-membrane and Membrane Biotechnology and Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education, College of Life Sciences, Peking University, Beijing 100871, China.
Zhigang Lu
Qinying Liu
Li Guo
He Ren
Jingyan Fu
Qing Jiang
Paul R Clarke
Chuanmao Zhang
Ministry of Education of the People's Republic of China · CNPeking University · CNUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G001480/1
6 · The paper itself

Abstract

The mechanism for nuclear envelope (NE) assembly is not fully understood. Importin-β and the small GTPase Ran have been implicated in the spatial regulation of NE assembly process. Here we report that chromatin-bound NLS (nuclear localization sequence) proteins provide docking sites for the NE precursor membrane vesicles and nucleoporins via importin-α and -β during NE assembly in Xenopus egg extracts. We show that along with the fast recruitment of the abundant NLS proteins such as nucleoplasmin and histones to the demembranated sperm chromatin in the extracts, importin-α binds the chromatin NLS proteins rapidly. Meanwhile, importin-β binds cytoplasmic NE precursor membrane vesicles and nucleoporins. Through interacting with importin-α on the chromatin NLS proteins, importin-β targets the membrane vesicles and nucleoporins to the chromatin surface. Once encountering Ran-GTP on the chromatin generated by RCC1, importin-β preferentially binds Ran-GTP and releases the membrane vesicles and nucleoporins for NE assembly. NE assembly is disrupted by blocking the interaction between importin-α and NLS proteins with excess soluble NLS proteins or by depletion of importin-β from the extract. Our findings reveal a novel molecular mechanism for NE assembly in Xenopus egg extracts.

Indexed as

alpha KaryopherinsAnimalsbeta KaryopherinsCell Cycle ProteinsChromatinGuanine Nucleotide Exchange FactorsHeLa CellsHumansNuclear EnvelopeNuclear Localization SignalsNuclear Pore Complex ProteinsNuclear Proteinsran GTP-Binding ProteinXenopusXenopus Proteinsalpha Karyopherinsbeta KaryopherinsCell Cycle ProteinsChromatinGuanine Nucleotide Exchange FactorsNuclear Localization SignalsNuclear Pore Complex ProteinsNuclear Proteinsran GTP-Binding ProteinRCC1 protein, XenopusXenopus Proteins

Identifiers

PMID22847741
PMCPMC3494395
OpenAlexW2069384357

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.