Dynamics of the Plant Nuclear Envelope and Nuclear Pore

Boruc, Joanna; Zhou, Xiao; Meier, Iris

doi:10.1104/pp.111.185256

Cited by 43 publications

(38 citation statements)

References 136 publications

(151 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In eukaryotes, macromolecular complexes larger than 40 to 60 kD are actively transported through NPCs, and therefore, gene-expression regulation requires a regulated and dynamic nucleocytoplasmic transport of molecules (Boruc et al, 2012;Field et al, 2014). The nascent premRNA transcripts recruit shuttling RNA-binding proteins, including SR proteins.…”

Section: Discussionmentioning

confidence: 99%

“…In plants, the regulation of mRNA export is far from being understood (Meier, 2012;Gaouar and Germain, 2013). Plant homologs of the mRNA transport adapter Nxf1-Nxt1 are not clearly identified and genes encoding those factors seem to be missing in plant genome (Serpeloni et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…Kap often binds to cargo molecules that carry either nuclear localization signals (NLS) for nuclear import or nuclear export signals (NES) for nuclear export (Boruc et al, 2012). The best-known import pathway is mediated by the importin-a/b Kap that binds to NLS.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Dynamic Distribution and Interaction of the Arabidopsis SRSF1 Subfamily Splicing Factors

Stankovic¹,

Schloesser²,

Joris³

et al. 2015

Plant Physiology

View full text Add to dashboard Cite

Ser/Arg-rich (SR) proteins are essential nucleus-localized splicing factors. Our prior studies showed that Arabidopsis (Arabidopsis thaliana) RSZ22, a homolog of the human SRSF7 SR factor, exits the nucleus through two pathways, either dependent or independent on the XPO1 receptor. Here, we examined the expression profiles and shuttling dynamics of the Arabidopsis SRSF1 subfamily (SR30, SR34, SR34a, and SR34b) under control of their endogenous promoter in Arabidopsis and in transient expression assay. Due to its rapid nucleocytoplasmic shuttling and high expression level in transient assay, we analyzed the multiple determinants that regulate the localization and shuttling dynamics of SR34. By site-directed mutagenesis of SR34 RNA-binding sequences and Arg/Ser-rich (RS) domain, we further show that functional RRM1 or RRM2 are dispensable for the exclusive protein nuclear localization and speckle-like distribution. However, mutations of both RRMs induced aggregation of the protein whereas mutation in the RS domain decreased the stability of the protein and suppressed its nuclear accumulation. Furthermore, the RNA-binding motif mutants are defective for their export through the XPO1 (CRM1/ Exportin-1) receptor pathway, but retain nucleocytoplasmic mobility. We performed a yeast two hybrid screen with SR34 as bait and discovered SR45 as a new interactor. SR45 is an unusual SR splicing factor bearing two RS domains. These interactions were confirmed in planta by FLIM-FRET and BiFC and the roles of SR34 domains in protein-protein interactions were further studied. Altogether, our report extends our understanding of shuttling dynamics of Arabidopsis SR splicing factors.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Dynamic Distribution and Interaction of the Arabidopsis SRSF1 Subfamily Splicing Factors

Stankovic¹,

Schloesser²,

Joris³

et al. 2015

Plant Physiology

View full text Add to dashboard Cite

show abstract

“…Nuclear pores regulate the movement of RNA, protein, and RNA-protein complexes into and out of the nucleus. The Update article from Meier and colleagues (Boruc et al, 2012) focuses on recent advances in elucidating the composition and dynamic organization of the nuclear envelopes and nuclear pore complexes. They further define their roles in selective nuclear import and export of macromolecules in plant cells.…”

Section: Nuclear Envelope and Nucleocytoplasmic Traffickingmentioning

confidence: 99%

Nuclear Architecture and Dynamics: Territories, Nuclear Bodies, and Nucleocytoplasmic Trafficking

Cheung

Reddy

2012

Plant Physiology

View full text Add to dashboard Cite

“…Although no lamin homologues have been identified in plants, the plant NPC might be anchored on the nuclear envelope in the same way as in vertebrates. Nuclear matrix constituent protein1 (NMCP1), which is a long coiled-coil protein localized at the nuclear rim, is considered to be the best candidate of plant lamin-like protein (Masuda et al, 1997;Boruc et al, 2012). Mutants of two NMCP1 homologues in Arabidopsis, little nuclei1 (linc1) and linc2, show reduced nuclear size and an altered nuclear structure (Dittmer et al, 2007).…”

Section: Ultrastructure Of the Plant Npcmentioning

confidence: 99%

The molecular architecture of the plant nuclear pore complex

Tamura¹,

Hara‐Nishimura²

2012

Journal of Experimental Botany

View full text Add to dashboard Cite

In mammals, cadmium is widely considered as a non-genotoxic carcinogen acting through a methylation-dependent epigenetic mechanism. Here, the effects of Cd treatment on the DNA methylation patten are examined together with its effect on chromatin reconfiguration in Posidonia oceanica. DNA methylation level and pattern were analysed in actively growing organs, under short-(6 h) and long-(2 d or 4 d) term and low (10 mM) and high (50 mM) doses of Cd, through a Methylation-Sensitive Amplification Polymorphism technique and an immunocytological approach, respectively. The expression of one member of the CHROMOMETHYLASE (CMT) family, a DNA methyltransferase, was also assessed by qRT-PCR. Nuclear chromatin ultrastructure was investigated by transmission electron microscopy. Cd treatment induced a DNA hypermethylation, as well as an up-regulation of CMT, indicating that de novo methylation did indeed occur. Moreover, a high dose of Cd led to a progressive heterochromatinization of interphase nuclei and apoptotic figures were also observed after long-term treatment. The data demonstrate that Cd perturbs the DNA methylation status through the involvement of a specific methyltransferase. Such changes are linked to nuclear chromatin reconfiguration likely to establish a new balance of expressed/repressed chromatin. Overall, the data show an epigenetic basis to the mechanism underlying Cd toxicity in plants.

show abstract

Dynamics of the Plant Nuclear Envelope and Nuclear Pore

Cited by 43 publications

References 136 publications

Dynamic Distribution and Interaction of the Arabidopsis SRSF1 Subfamily Splicing Factors

Dynamic Distribution and Interaction of the Arabidopsis SRSF1 Subfamily Splicing Factors

Nuclear Architecture and Dynamics: Territories, Nuclear Bodies, and Nucleocytoplasmic Trafficking

The molecular architecture of the plant nuclear pore complex

Contact Info

Product

Resources

About