SnapShot: Nucleo-cytoskeletal Interactions

Janota, Cátia S.; Calero-Cuenca, Francisco J.; Costa, Jerome; Gomes, Edgar R.

doi:10.1016/j.cell.2017.05.014

Cited by 18 publications

(13 citation statements)

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“…The nature of the cytoskeletal elements that act upstream of the LINC complex in myofibers is not clear. The elaborate MT cytoskeleton that surrounds each myonucleus postulated previously to transmit mechanical signals into the nuclei ( Hampoelz et al, 2011 ; Janota et al, 2017 ) appear to be less relevant to cell-cycle regulation. Moreover, our results imply that the MT cytoskeleton is not primarily involved in maintenance of nuclear position in mature myofibers, although extremely prolonged inhibition of the MT network in these cells (>3 d) did perturb both sarcomere organization and nuclear position in larval muscles (unpublished data).…”

Section: Discussionmentioning

confidence: 93%

“…Cytoplasmic mechanical inputs are transmitted across the nuclear membrane by the linker of nucleoskeleton and cytoskeleton (LINC) complex, composed of cytoplasmic components of the Nesprin-family members ( Wang et al, 2009 ; Rajgor and Shanahan, 2013 ; Chang et al, 2015 ; Meinke and Schirmer, 2015 ; Janota et al, 2017 ). These components are associated with the cytoplasmic cytoskeleton as well as with the outer nuclear membrane through their klarsicht, ANC-1, syne homology (KASH) domain.…”

Section: Introductionmentioning

confidence: 99%

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Mechanotransduction via the LINC complex regulates DNA replication in myonuclei

Wang

Stoops

et al. 2018

Journal of Cell Biology

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Section: Discussionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Mechanotransduction via the LINC complex regulates DNA replication in myonuclei

Wang

Stoops

et al. 2018

Journal of Cell Biology

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“…The LINC complex is the main player connecting the nucleus to the cytoskeleton and it has an essential role for nuclear movement and positioning [10,11,33]. In order to identify new regulators of nuclear position we tested the involvement of Ctdnep1, a nuclear envelope and endoplasmic reticulum Ser/Thr phosphatase in polarization of migrating cells [40,52].…”

Section: Resultsmentioning

confidence: 99%

“…The nucleus is permanently under tension from different intracellular forces that result from nucleo-cytoskeletal connections and regulate nuclear movement and mechanotransduction [8–10]. These connections are mainly mediated by the Linker of Nucleoskeleton and Cytoskeleton (LINC) complex, located at the nuclear envelope [11,12]. The LINC complex is composed of KASH domain proteins (Nesprins in mammals) at the outer nuclear membrane that bind to SUN domain proteins, located at the inner nuclear membrane.…”

Section: Introductionmentioning

confidence: 99%

Ctdnep1 and Eps8L2 regulate dorsal actin cables for nuclear positioning during cell migration

Calero-Cuenca

Osório

Sridhara

et al. 2020

Preprint

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SummaryCells actively position their nuclei within the cytoplasm for multiple cellular and physiological functions. Different cell types position their nuclei away from the leading edge to migrate properly. In migrating fibroblasts, nuclear positioning is driven by dorsal actin cables connected to the nuclear envelope by the LINC complex on Transmembrane Actin-associated Nuclear (TAN) lines. How dorsal actin cables are organized to form TAN lines is unknown. Here, we report a role for Ctdnep1/Dullard, a nuclear envelope phosphatase, and the actin regulator Eps8L2, on nuclear positioning. We demonstrate that Ctdnep1 and Eps8L2 directly interact to regulate the formation and thickness of dorsal actin cables required for TAN lines engagement for nuclear positioning. Our work establishes a novel mechanism to locally regulate actin at the nuclear envelope for nuclear positioning.

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“…KASH proteins are positioned on the cytoplasmic surface of the nuclear envelope where they can interact with a variety of different cytoskeletal modules. 24,80 The KASH protein UNC-83 interacts with microtubule motors to move nuclei. A yeast two-hybrid screen with the cytoplasmic domain of UNC-83 identified interactions between UNC-83 and four regulators of microtubule motors: the kinesin light chain KLC-2, and the dynein regulators NUD-2 (NudE homolog), BICD-1 (bicaudalD homolog), and DLC-1 (an LC8 dynein light chain).…”

Section: Unc-84/unc-83 Linc Complexes Recruit Microtubule Motors To Mmentioning

confidence: 99%

A network of nuclear envelope proteins and cytoskeletal force generators mediates movements of and within nuclei throughoutCaenorhabditis elegansdevelopment

Starr

2019

Exp Biol Med (Maywood)

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Nuclear migration and anchorage, together referred to as nuclear positioning, are central to many cellular and developmental events. Nuclear positioning is mediated by a conserved network of nuclear envelope proteins that interacts with force generators in the cytoskeleton. At the heart of this network are linker of nucleoskeleton and cytoskeleton (LINC) complexes made of Sad1 and UNC-84 (SUN) proteins at the inner nuclear membrane and Klarsicht, ANC-1, and Syne homology (KASH) proteins in the outer nuclear membrane. LINC complexes span the nuclear envelope, maintain nuclear envelope architecture, designate the surface of nuclei distinctly from the contiguous endoplasmic reticulum, and were instrumental in the early evolution of eukaryotes. LINC complexes interact with lamins in the nucleus and with various cytoplasmic KASH effectors from the surface of nuclei. These effectors regulate the cytoskeleton, leading to a variety of cellular outputs including pronuclear migration, nuclear migration through constricted spaces, nuclear anchorage, centrosome attachment to nuclei, meiotic chromosome movements, and DNA damage repair. How LINC complexes are regulated and how they function are reviewed here. The focus is on recent studies elucidating the best-understood network of LINC complexes, those used throughout Caenorhabditis elegans development. Impact statement Defects in nuclear positioning disrupt development in many mammalian tissues. In human development, LINC complexes play important cellular functions including nuclear positioning, homolog pairing in meiosis, DNA damage repair, wound healing, and gonadogenesis. The topics reviewed here are relevant to public health because defects in nuclear positioning and mutations in LINC components are associated with a wide variety of human diseases including muscular dystrophies, neurological disorders, progeria, aneurysms, hearing loss, blindness, sterility, and multiple cancers. Although this review focuses on findings in the model nematode Caenorhabditis elegans, the studies are relevant because almost all the findings originally made in C. elegans are conserved to humans. Furthermore, C. elegans remains the best described network for how LINC complexes are regulated and function.

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SnapShot: Nucleo-cytoskeletal Interactions

Abstract: The nucleus is connected to the cytoskeleton, and these connections are involved in multiple functions such as nuclear positioning, shape and stiffness, cytoskeleton organization, mechanotransduction, gene expression, chromosome positioning, DNA repair, and cell migration.

Cited by 18 publications

References 0 publications

Mechanotransduction via the LINC complex regulates DNA replication in myonuclei

Mechanotransduction via the LINC complex regulates DNA replication in myonuclei

Ctdnep1 and Eps8L2 regulate dorsal actin cables for nuclear positioning during cell migration

A network of nuclear envelope proteins and cytoskeletal force generators mediates movements of and within nuclei throughoutCaenorhabditis elegansdevelopment

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