Lamin-like analogues in plants: the characterization of NMCP1 in Allium cepa

Ciska, Malgorzata; Masuda, Kiyoshi; Espina, Susana Moreno Dı́az de la

doi:10.1093/jxb/ert020

Cited by 63 publications

(96 citation statements)

References 38 publications

(75 reference statements)

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“…ABSCISIC ACID INSENSITIVE3 (ABI3), a key transcription factor in seed maturation, participates in nuclear shrinkage which is thought to be a general adaptive response to desiccation tolerance [van Zanten et al, 2011]. During the early events of seed germination (48-72 h after imbibition), the nuclear volume increases again, and this increase requires the activity of LITTLE NUCLEI1 (LINC1) and LINC2, 2 lamin-like analogues [van Zanten et al, 2011[van Zanten et al, , 2012bCiska et al, 2013]. Furthermore, chromatin reorganization accompanies this event.…”

Section: Dynamics Of the Heterochromatin Compartment During Developmentmentioning

confidence: 99%

Nuclear Architecture and Chromatin Dynamics in Interphase Nuclei of Arabidopsis thaliana

Prete

Arpòn

Sakai

et al. 2014

Cytogenet Genome Res

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The interphase cell nucleus is extraordinarily complex, ordered, and dynamic. In the last decade, remarkable progress has been made in deciphering the functional organisation of the cell nucleus, and intricate relationships between genome functions (transcription, DNA repair, or replication) and various nuclear compartments have been revealed. In this review, we describe the architecture of the Arabidopsis thaliana interphase cell nucleus and discuss the dynamic nature of its organisation. We underline the need for further developments in quantitative and modelling approaches to nuclear organization.

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Section: Dynamics Of the Heterochromatin Compartment During Developmentmentioning

confidence: 99%

Nuclear Architecture and Chromatin Dynamics in Interphase Nuclei of Arabidopsis thaliana

Prete

Arpòn

Sakai

et al. 2014

Cytogenet Genome Res

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“…14 However, no lamin homologs have been found in plant proteomes. 15 Instead, Nuclear Matrix Constituent Proteins (NMCP) [16][17][18] and their Arabidopsis homologs, CROWDED NUCLEI (CRWN, also known as LITTLE NUCLEI) proteins, were identified as putative analogs of mammalian lamins in plants. 15 NMCP/CRWN proteins are coiled-coil proteins isolated from plant nuclear fractions and are proposed to share structural similarity to lamins.…”

Section: Introductionmentioning

confidence: 99%

Plant nuclear shape is independently determined by the SUN-WIP-WIT2-myosin XI-i complex and CRWN1

Zhou

Groves

Meier

2015

Nucleus

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Nuclei undergo dynamic shape changes during plant development, but the mechanism is unclear. In Arabidopsis, Sad1/UNC-84 (SUN) proteins, WPP domain-interacting proteins (WIPs), WPP domain-interacting tail-anchored proteins (WITs), myosin XI-i, and CROWDED NUCLEI 1 (CRWN1) have been shown to be essential for nuclear elongation in various epidermal cell types. It has been proposed that WITs serve as adaptors linking myosin XI-i to the SUN-WIP complex at the nuclear envelope (NE). Recently, an interaction between Arabidopsis SUN1 and SUN2 proteins and CRWN1, a plant analog of lamins, has been reported. Therefore, the CRWN1-SUN-WIP-WIT-myosin XI-i interaction may form a linker of the nucleoskeleton to the cytoskeleton complex. In this study, we investigate this proposed mechanism in detail for nuclei of Arabidopsis root hairs and trichomes. We show that WIT2, but not WIT1, plays an essential role in nuclear shape determination by recruiting myosin XI-i to the SUN-WIP NE bridges. Compared with SUN2, SUN1 plays a predominant role in nuclear shape. The NE localization of SUN1, SUN2, WIP1, and a truncated WIT2 does not depend on CRWN1. While crwn1 mutant nuclei are smooth, the nuclei of sun or wit mutants are invaginated, similar to the reported myosin XI-i mutant phenotype. Together, this indicates that the roles of the respective WIT and SUN paralogs have diverged in trichomes and root hairs, and that the SUN-WIP-WIT2-myosin XI-i complex and CRWN1 independently determine elongated nuclear shape. This supports a model of nuclei being shaped both by cytoplasmic forces transferred to the NE and by nucleoplasmic filaments formed under the NE.

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“…These proteins have a tripartite structure with a central coiled coil domain, and they are predicted to dimerize and probably form filaments like lamins (Masuda et al, 1999; Dittmer et al, 2007; Ciska et al, 2013; Ciska and Moreno Díaz de la Espina, 2013). They also participate in the nuclear functions mediated by lamins, such as the regulation of nuclear shape and size, and heterochromatin organization (Dittmer et al, 2007; Dittmer and Richards, 2008; van Zanten et al, 2011, 2012; Sakamoto and Takagi, 2013; Wang et al, 2013).…”

Section: Protein Components Of the Plant Laminamentioning

confidence: 99%

The intriguing plant nuclear lamina

Ciska

Espina

2014

Front. Plant Sci.

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The nuclear lamina is a complex protein mesh attached to the inner nuclear membrane (INM), which is also associated with nuclear pore complexes. It provides mechanical support to the nucleus and nuclear envelope, and as well as facilitating the connection of the nucleoskeleton to the cytoskeleton, it is also involved in chromatin organization, gene regulation, and signaling. In metazoans, the nuclear lamina consists of a polymeric layer of lamins and other interacting proteins responsible for its association with the INM and chromatin. In plants, field emission scanning electron microscopy of nuclei, and thin section transmission electron microscopy of isolated nucleoskeletons, reveals the lamina to have a similar structure to that of metazoans. Moreover, although plants lack lamin genes and the genes encoding most lamin-binding proteins, the main functions of the lamina are fulfilled in plants. Hence, it would appear that the plant lamina is not based on lamins and that other proteins substitute for lamins in plant cells. The nuclear matrix constituent proteins are the best characterized structural proteins in the plant lamina. Although these proteins do not display strong sequence similarity to lamins, their predicted secondary structure and sub-nuclear distribution, as well as their influence on nuclear size and shape, and on heterochromatin organization, suggest they could be functional lamin analogs. In this review we shall summarize what is currently known about the organization and composition of the plant nuclear lamina and its interacting complexes, and we will discuss the activity of this structure in the plant cell and its nucleus.

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Lamin-like analogues in plants: the characterization of NMCP1 in Allium cepa

Cited by 63 publications

References 38 publications

Nuclear Architecture and Chromatin Dynamics in Interphase Nuclei of <b><i>Arabidopsis thaliana</i></b>

Nuclear Architecture and Chromatin Dynamics in Interphase Nuclei of <b><i>Arabidopsis thaliana</i></b>

Plant nuclear shape is independently determined by the SUN-WIP-WIT2-myosin XI-i complex and CRWN1

The intriguing plant nuclear lamina

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