The Nuclear Envelope — Structure and Protein Interactions

Graumann, Katja; Evans, David

doi:10.1002/9781118472507.ch2

Cited by 8 publications

(5 citation statements)

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“…Only guard cell pairs with a major axis of the rendered ellipse longer than 8 µm were measured. To avoid stomatal aperture effects on nuclear position, cell, and this involves migration of the nucleus toward the infection site (Gross et al, 1993;Skalamera and Heath, 1998;Schmelzer, 2002;Caillaud et al, 2012;Graumann and Evans, 2013). To suppress plant immunity, pathogens translocate effector proteins into host cells, several of which are targeted to the host cell nucleus (Deslandes and Rivas, 2011).…”

Section: Sine1 Is Associated With F-actin Through Its Arm Repeatsmentioning

confidence: 99%

Identification of unique SUN-interacting nuclear envelope proteins with diverse functions in plants

Zhou

Graumann

Wirthmueller

et al. 2014

Journal of Cell Biology

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Section: Sine1 Is Associated With F-actin Through Its Arm Repeatsmentioning

confidence: 99%

Identification of unique SUN-interacting nuclear envelope proteins with diverse functions in plants

Zhou

Graumann

Wirthmueller

et al. 2014

Journal of Cell Biology

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“…Cter-SUNs contain a SUN domain at the C-terminal part of the protein while the mid-SUN proteins have a central (mid) SUN domain (figure 2A)(Graumann and Evans 2013a). In Arabidopsis, Cter-SUNs are the most studied although mid-SUNs were described in other organisms from yeast to human(Murphy et al 2010;Sohaskey et al 2010;Field et al 2012;Friederichs et al 2012).…”

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confidence: 99%

The plant LINC complex at the nuclear envelope

et al. 2014

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Significant advances in understanding the plant nuclear envelope have been made over the past few years; indeed, knowledge of the protein network at the nuclear envelope is rapidly growing. One such network, the linker of nucleoskeleton and cytoskeleton (LINC) complex, is known in animals to connect chromatin to the cytoskeleton through the nuclear envelope. The LINC complex is made of Sad1/Unc84 (SUN) and Klarsicht/Anc1/Syne1 homology (KASH) proteins which have been recently characterized in plants. SUN proteins are located within the inner nuclear membrane, while the KASH proteins are included into the outer nuclear membrane. SUN and KASH domains interact and bridge the two nuclear membranes. In Arabidopsis, KASH proteins also interact with the tryptophan-proline-proline (WPP) domain-interacting tail-anchored protein 1 (WIT1), associated with the nuclear pore complex and with myosin XI-i which directly interacts with the actin cytoskeleton. Although evidence for a plant LINC complex connecting the nucleus to the cytoskeleton is growing, its interaction with chromatin is still unknown, but knowledge gained from animal models strongly suggests its existence in plants. Possible functions of the plant LINC complex in cell division, nuclear shape, and chromatin organization are discussed.

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“…During cell cycle progression in eukaryotes, the intrinsic localization of centrosomes in the nuclear envelope is orchestrated by microtubules under the influence of dynein motor proteins. 49 , 50 Previous studies showed that dyneins act in association with dynactin via the microtubule-spindle pole network to partly mediate the disappearance of nuclear membranes by pulling the spindle poles toward opposite ends of the cell. 51 , 52 We demonstrated that targeted gene disruption of MoDYNC1I2 in the rice blast fungus triggered abnormal nuclear distribution.…”

Section: Discussionmentioning

confidence: 99%