Shaping the nucleus: Factors and forces

Walters, Alison D.; Bommakanti, Ananth; Cohen-Fix, Orna

doi:10.1002/jcb.24178

Cited by 74 publications

(65 citation statements)

References 91 publications

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“…The nuclear envelope is comprised of an inner and an outer nuclear membrane, the latter of which is contiguous with the endoplasmic reticulum of the cytoplasm. 1,2,14 The inner and outer nuclear membranes are connected by structures measuring about 100-150 nm in diameter known as nuclear pore complexes (NPCs) that span the nuclear envelope. It is the NPCs that allow passage of molecules between cytoplasm and nucleus.…”

Section: Nuclear Trafficmentioning

confidence: 99%

STATs get their move on

Reich¹

2013

JAK-STAT

110

103

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Section: Nuclear Trafficmentioning

confidence: 99%

STATs get their move on

Reich¹

2013

JAK-STAT

110

103

View full text Add to dashboard Cite

“…A fundamental question in cell biology is how the sizes of intracellular structures and organelles are regulated relative to cell size (Rafelski and Marshall, 2008;Chan and Marshall, 2012;Levy and Heald, 2012;Marshall, 2012). It has long been noted that the size of the nucleus tends to correlate with the size of the cell, a phenomenon referred to as nuclear scaling (Conklin, 1912;Wilson, 1925;Webster et al, 2009;Chan and Marshall, 2010;Levy and Heald, 2010;Walters et al, 2012;Hara et al, 2013;. Altered nuclear scaling is associated with many cancers, and cytopathologists monitor graded increases in nuclear size for cancer diagnosis and prognosis (Zink et al, 2004;Chow et al, 2012;.…”

Section: Introductionmentioning

confidence: 99%

Nuclear size is sensitive to NTF2 protein levels in a manner dependent on Ran binding

Vuković

Jevtić

Zhang

et al. 2016

Journal of Cell Science

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Altered nuclear size is associated with many cancers, and determining whether cancer-associated changes in nuclear size contribute to carcinogenesis necessitates an understanding of mechanisms of nuclear size regulation. Although nuclear import rates generally positively correlate with nuclear size, NTF2 levels negatively affect nuclear size, despite the role of NTF2 (also known as NUTF2) in nuclear recycling of the import factor Ran. We show that binding of Ran to NTF2 is required for NTF2 to inhibit nuclear expansion and import of large cargo molecules in Xenopus laevis egg and embryo extracts, consistent with our observation that NTF2 reduces the diameter of the nuclear pore complex (NPC) in a Ranbinding-dependent manner. Furthermore, we demonstrate that ectopic NTF2 expression in Xenopus embryos and mammalian tissue culture cells alters nuclear size. Finally, we show that increases in nuclear size during melanoma progression correlate with reduced NTF2 expression, and increasing NTF2 levels in melanoma cells is sufficient to reduce nuclear size. These results show a conserved capacity for NTF2 to impact on nuclear size, and we propose that NTF2 might be a new cancer biomarker.

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“…Nuclear shapes in mammals are also controlled by the nuclear lamina components, including the lamin proteins (Sullivan et al, 1999;Goldman et al, 2004;Prüfert et al, 2004Prüfert et al, , 2005Lammerding et al, 2006;Volkova et al, 2011) and the lamin binding protein Titin (Zastrow et al, 2006). Although many factors affect nuclear morphology (Walters et al, 2012), the nuclear lamina seems to be the major contributor to maintenance of the nuclear shape (Webster et al, 2009). Hence, focusing on nuclear shape would make it possible to identify lamina components.…”

Section: Introductionmentioning

confidence: 99%

The Novel Nuclear Envelope Protein KAKU4 Modulates Nuclear Morphology inArabidopsis

et al. 2014

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In animals, the nuclear lamina is a fibrillar meshwork on the inner surface of the nuclear envelope, composed of coiled-coil lamin proteins and lamin binding membrane proteins. Plants also have a meshwork on the inner surface of the nuclear envelope, but little is known about its composition other than the presence of members of the CROWDED NUCLEI (CRWN) protein family, possible plant lamin analogs. Here, we describe a candidate lamina component, based on two Arabidopsis thaliana mutants (kaku2 and kaku4) with aberrant nuclear morphology. The responsible gene in kaku2 encodes CRWN1, and the responsible gene in kaku4 encodes a plant-specific protein of unknown function (KAKU4) that physically interacts with CRWN1 and its homolog CRWN4. Immunogold labeling revealed that KAKU4 localizes at the inner nuclear membrane. KAKU4 deforms the nuclear envelope in a dose-dependent manner, in association with nuclear membrane invagination and stack formation. The KAKU4-dependent nuclear envelope deformation was enhanced by overaccumulation of CRWN1, although KAKU4 can deform the nuclear envelope even in the absence of CRWN1 and/or CRWN4. Together, these results suggest that plants have evolved a unique lamina-like structure to modulate nuclear shape and size.

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Shaping the nucleus: Factors and forces

Cited by 74 publications

References 91 publications

STATs get their move on

STATs get their move on

Nuclear size is sensitive to NTF2 protein levels in a manner dependent on Ran binding

The Novel Nuclear Envelope Protein KAKU4 Modulates Nuclear Morphology inArabidopsis

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