Subnuclear compartmentalization and function of actin and nuclear Myosin I in plants

Cruz, José Ramón Alvero; Espina, Susana Moreno Dı́az de la

doi:10.1007/s00412-008-0188-y

Cited by 37 publications

(34 citation statements)

References 65 publications

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“…Although reports of endogenous nuclear ARP2/3 are rare, our results are consistent with previous reports that other plant ARP2/3 pathway components and actin have been detected in the nucleus (Cruz and Moreno Diaz de la Espina, 2008; Zhang et al, 2010; Dyachok et al, 2011). Historically in the actin field, the topic of F-actin in the nucleus in general has been controversial, and the precise function of nuclear ARP2/3 is not known (Goley et al, 2006; Yoo et al, 2007).…”

Section: Discussionsupporting

confidence: 93%

ARP2/3 localization in Arabidopsis leaf pavement cells: a diversity of intracellular pools and cytoskeletal interactions

Zhang¹,

Mallery²,

Szymanski³

2013

Front. Plant Sci.

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In plant cells the actin cytoskeleton adopts many configurations, but is best understood as an unstable, interconnected track that rearranges to define the patterns of long distance transport of organelles during growth. Actin filaments do not form spontaneously; instead filament nucleators, such as the evolutionarily conserved actin-related protein (ARP) 2/3 complex, can efficiently generate new actin filament networks when in a fully activated state. A growing number of genetic experiments have shown that ARP2/3 is necessary for morphogenesis in processes that range from tip growth during root nodule formation to the diffuse polarized growth of leaf trichomes and pavement cells. Although progress has been rapid in the identification of proteins that function in series to positively regulate ARP2/3, less has been learned about the actual function of ARP2/3 in cells. In this paper, we analyze the localization of ARP2/3 in Arabidopsis leaf pavement cells. We detect a pool of ARP2/3 in the nucleus, and also find that ARP2/3 is efficiently and specifically clustered on multiple organelle surfaces and associates with both the actin filament and microtubule cytoskeletons. Our mutant analyses and ARP2/3 and actin double labeling experiments indicate that the clustering of ARP2/3 on organelle surfaces and an association with actin bundles does not necessarily reflect an active pool of ARP2/3, and instead most of the complex appears to exist as a latent organelle-associated pool.

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Section: Discussionsupporting

confidence: 93%

ARP2/3 localization in Arabidopsis leaf pavement cells: a diversity of intracellular pools and cytoskeletal interactions

Zhang¹,

Mallery²,

Szymanski³

2013

Front. Plant Sci.

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“…The high degree of sequence conservation renders actin a poor immunogen. However, a small number of antibodies exist that recognize conformational actin epitopes (Gonsior et al, 1999;Schoenenberger et al, 2005), We and others have shown that such antibodies reveal distinct actin structures in the nucleus and cytoplasm (Cruz and Moreno Diaz de la Espina, 2008). Although one of these antibodies, monoclonal 1C7, was raised against crosslinked LD, it recognizes an epitope that is not specific to LD (see Fig.…”

Section: Discussionmentioning

confidence: 96%

An antiparallel actin dimer is associated with the endocytic pathway in mammalian cells

Silván

Boiteux

Sütterlin

et al. 2012

Journal of Structural Biology

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“…A considerable body of data is available about the involvement of actin and nuclear myosin I in transcription by RNA polymerase I as well as in some later steps of ribosome biogenesis (Cisterna et al 2009(Cisterna et al , 2006Cruz and Moreno Diaz de la Espina 2009;Fomproix and Percipalle 2004;Obrdlik et al 2010;Percipalle et al 2006;Philimonenko et al 2004;Ye et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Transcription-dependent rearrangements of actin and nuclear myosin I in the nucleolus

Philimonenko

Janáček

Harata

et al. 2010

Histochem Cell Biol

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Nuclear actin and nuclear myosin I (NMI) are important players in transcription of ribosomal genes. Transcription of rDNA takes place in highly organized intranuclear compartment, the nucleolus. In this study, we characterized the localization of these two proteins within the nucleolus of HeLa cells with high structural resolution by means of electron microscopy and gold-immunolabeling. We demonstrate that both actin and NMI are localized in specific compartments within the nucleolus, and the distribution of NMI is transcription-dependent. Moreover, a pool of NMI is present in the foci containing nascent rRNA transcripts. Actin, in turn, is present both in transcriptionally active and inactive regions of the nucleolus and colocalizes with RNA polymerase I and UBF. Our data support the involvement of actin and NMI in rDNA transcription and point out to other functions of these proteins in the nucleolus, such as rRNA maturation and maintenance of nucleolar architecture.

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Subnuclear compartmentalization and function of actin and nuclear Myosin I in plants

Cited by 37 publications

References 65 publications

ARP2/3 localization in Arabidopsis leaf pavement cells: a diversity of intracellular pools and cytoskeletal interactions

ARP2/3 localization in Arabidopsis leaf pavement cells: a diversity of intracellular pools and cytoskeletal interactions

An antiparallel actin dimer is associated with the endocytic pathway in mammalian cells

Transcription-dependent rearrangements of actin and nuclear myosin I in the nucleolus

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