SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton

Tzur, Yonatan B; Wilson, Katherine L.; Gruenbaum, Yosef

doi:10.1038/nrm2003

Cited by 220 publications

(226 citation statements)

References 56 publications

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“…2; for review see 6,[13][14][15]. In general, SUN proteins contain a conserved SUN domain at their C-termini and at least one transmembrane domain.…”

Section: Kash and Sun Proteins Bridge The Nuclear Envelopementioning

confidence: 99%

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Communication between the cytoskeleton and the nuclear envelope to position the nucleus

Starr

2007

Mol. BioSyst.

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In most eukaryotic cells, the nucleus is localized to a specific location. This highlight article focuses on recent advances describing the mechanisms of nuclear migration and anchorage. Central to nuclear positioning mechanisms is the communication between the nuclear envelope and the cytoskeleton. All three components of the cytoskeleton-microtubules, actin filaments and intermediate filaments -are involved in nuclear positioning to varying degrees in different cell types. KASH proteins on the outer nuclear membrane connect to SUN proteins on the inner nuclear membrane. Together they transfer forces between the cytoskeleton and the nuclear lamina. Once at the outer nuclear membrane, KASH proteins can interact with the cytoskeleton. Nuclear migrations are a component of many cellular migration events and defects in nuclear positioning lead to human diseases, most notably lissencephaly.

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“…2; for review see 6,[13][14][15]. In general, SUN proteins contain a conserved SUN domain at their C-termini and at least one transmembrane domain.…”

Section: Kash and Sun Proteins Bridge The Nuclear Envelopementioning

confidence: 99%

“…2; for review see ref. 6,[13][14][15]. The nuclear envelope bridging model has been refined by four groups who have each concluded that SUN proteins reside in the INM where they function to target and retain KASH proteins to the ONM through a direct interaction.…”

Section: Kash and Sun Proteins Bridge The Nuclear Envelopementioning

confidence: 99%

Communication between the cytoskeleton and the nuclear envelope to position the nucleus

Starr

2007

Mol. BioSyst.

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“…Mps3 contains a SUN domain (Sad1-Unc84) within its inter-membrane region which allows it to connect the SPB with the nuclear envelope. 25,26 Mps3 is the only SUN domain protein in budding yeast, while at least two SUN domain proteins exist in C. elegans and Drosophlila, and mammalian cells have four SUN domain proteins. In the latter case, SUN domains are known to interact with the KASH domain of outer nuclear membrane proteins, such as Nesprin, bridging the nuclear envelope to the actin cytoskeleton.…”

Section: Introductionmentioning

confidence: 99%

Opening the DNA repair toolbox: Localization of DNA double strand breaks to the nuclear periphery

Oza¹,

Peterson²

2010

Cell Cycle

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E fficient repair of DNA double strand breaks is essential for cells to avoid increased mutation rates, genomic instability, and even cell death. Consequently, cells have evolved multiple mechanisms for rapidly repairing these DNA lesions, including error-free homologous recombination as well as error-prone pathways such as nonhomologous end joining. What happens to DSBs that are repaired inefficiently or not at all? Recently, several studies in budding yeast have shown that these more recalcitrant DSBs are localized to the nuclear periphery through interactions between the nuclear envelope protein, Mps3, and proteins associated with DSB chromatin. Why these DSBs are tethered to the nuclear periphery is still not clear, though the current view is that alternative repair pathways may be activated at the periphery in a final attempt to repair the lesion. In this Extra View, we discuss these recent reports, and we show that the Est1 component of the telomerase machinery plays an essential role in anchoring DSB chromatin to the nuclear envelope protein, Mps3.

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“…At the cell surface, IF interact with desmosomes, hemidesmosomes, focal adhesions and the extracellular matrix via a variety of linker proteins [3][4][5]. There is also evidence that IF associate with factors on the outer nuclear membrane which, in turn, connect to components of the nuclear lamina [4,6]. These observations suggest that IF form a continuous network of nanofibrils along which signals from the cell's exterior can be transmitted to the nuclear surface and the nucleoplasm.…”

Section: Introductionmentioning

confidence: 99%

“…The extensive distribution of IF provides an enormous surface area which can act as a scaffold for the binding of numerous types of regulatory and signaling molecules [8,9]. The IF system has also been shown to associate with membranous organelles such as mitochondria, the Golgi apparatus and vesicles, as well as with other cytoskeletal components such as actin filaments, microtubules, and their associated molecular motors [4,6,10]. Thus the IF system is positioned to perform significant roles in the internal organization and positioning of organelles and other cytoplasmic components.…”

Section: Introductionmentioning

confidence: 99%

Intermediate filaments: versatile building blocks of cell structure

Goldman

Grin

Mendez

et al. 2008

Current Opinion in Cell Biology

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SummaryCytoskeletal intermediate filaments (IF) are organized into a dynamic nano-fibrillar complex that extends throughout mammalian cells. This organization is ideally suited to their roles as response elements in the subcellular transduction of mechanical perturbations initiated at cell surfaces. IF also provide a scaffold for other types of signal transduction which together with molecular motors ferries signaling molecules from the cell periphery to the nucleus. Recent insights into their assembly highlight the importance of co-translation of their precursors, the hierarchical organization of their subunits in the formation of unit length filaments (ULF), and the linkage of ULF into mature apolar IF. Analyses by atomic force microscopy reveal that mature IF are flexible and can be stretched to over 300% of their length without breaking, suggesting that intrafilament subunits can slide past one another when exposed to mechanical stress and strain. IF also play a role in the organization of organelles by modulating their motility and providing anchorage sites within the cytoplasm.

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SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton

Cited by 220 publications

References 56 publications

Communication between the cytoskeleton and the nuclear envelope to position the nucleus

Communication between the cytoskeleton and the nuclear envelope to position the nucleus

Opening the DNA repair toolbox: Localization of DNA double strand breaks to the nuclear periphery

Intermediate filaments: versatile building blocks of cell structure

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