Drosophila KASH-domain protein Klarsicht regulates microtubule stability and integrin receptor localization during collective cell migration

Myat, Monn Monn; Rashmi, R.N.; Manna, Dipak; Xu, Na; Patel, Unisha; Galiano, Michael; Zieliński, K; Lam, Aaron; Welte, Michael A.

doi:10.1016/j.ydbio.2015.08.003

Cited by 10 publications

(9 citation statements)

References 49 publications

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“…They also showed that nesprin-1α regulates MT nucleation [100]. In Drosophila , KASH domain protein Klarsicht regulates MT stability and integrin localization during collective cell migration [101]. These results indicate a physical role for the nucleus as anchoring point for cytoplasmic cytoskeletal elements.…”

Section: Effects Of Ne On the Cytosolic Cytoskeletonmentioning

confidence: 99%

Signal Transduction across the Nuclear Envelope: Role of the LINC Complex in Bidirectional Signaling

Hieda

2019

Cells

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The primary functions of the nuclear envelope are to isolate the nucleoplasm and its contents from the cytoplasm as well as maintain the spatial and structural integrity of the nucleus. The nuclear envelope also plays a role in the transfer of various molecules and signals to and from the nucleus. To reach the nucleus, an extracellular signal must be transmitted across three biological membranes: the plasma membrane, as well as the inner and outer nuclear membranes. While signal transduction across the plasma membrane is well characterized, signal transduction across the nuclear envelope, which is essential for cellular functions such as transcriptional regulation and cell cycle progression, remains poorly understood. As a physical entity, the nuclear envelope, which contains more than 100 proteins, functions as a binding scaffold for both the cytoskeleton and the nucleoskeleton, and acts in mechanotransduction by relaying extracellular signals to the nucleus. Recent results show that the Linker of Nucleoskeleton and Cytoskeleton (LINC) complex, which is a conserved molecular bridge that spans the nuclear envelope and connects the nucleoskeleton and cytoskeleton, is also capable of transmitting information bidirectionally between the nucleus and the cytoplasm. This short review discusses bidirectional signal transduction across the nuclear envelope, with a particular focus on mechanotransduction.

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Section: Effects Of Ne On the Cytosolic Cytoskeletonmentioning

confidence: 99%

Signal Transduction across the Nuclear Envelope: Role of the LINC Complex in Bidirectional Signaling

Hieda

2019

Cells

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“…g-TURC is released from the centriole in a spastin-dependent manner and is then anchored to the apical membrane through the transmembrane protein Piopio. As embryogenesis proceeds and salivary gland and tracheal cells migrate collectively to form tubes, MTs become progressively stabilized and extend along the apicobasal axis (Brodu et al 2010;Myat et al 2015).…”

Section: Microtubule Organization and Motor Proteins In Animal Tissuementioning

confidence: 99%

Microtubule Motors in Establishment of Epithelial Cell Polarity

Kreitzer

Myat

2017

Cold Spring Harb Perspect Biol

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Epithelial cells play a key role in insuring physiological homeostasis by acting as a barrier between the outside environment and internal organs. They are also responsible for the vectorial transport of ions and fluid essential to the function of many organs. To accomplish these tasks, epithelial cells must generate an asymmetrically organized plasma membrane comprised of structurally and functionally distinct apical and basolateral membranes. Adherent and occluding junctions, respectively, anchor cells within a layer and prevent lateral diffusion of proteins in the outer leaflet of the plasma membrane and restrict passage of proteins and solutes through intercellular spaces. At a fundamental level, the establishment and maintenance of epithelial polarity requires that signals initiated at cell-substratum and cell-cell adhesions are transmitted appropriately and dynamically to the cytoskeleton, to the membrane-trafficking machinery, and to the regulation of occluding and adherent junctions. Rigorous descriptive and mechanistic studies published over the last 50 years have provided great detail to our understanding of epithelial polarization. Yet still, critical early steps in morphogenesis are not yet fully appreciated. In this review, we discuss how cytoskeletal motor proteins, primarily kinesins, contribute to coordinated modification of microtubule and actin arrays, formation and remodeling of cell adhesions to targeted membrane trafficking, and to initiating the formation and expansion of an apical lumen.

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“…Importantly, both the AKT and the profibrotic TGFβ pathways that drive cardiac hypertrophy and interstitial fibrosis are mechanoresponsive, largely through pathways sensitive to inputs from cellular adhesions and/or the state of the actomyosin cytoskeleton (Iijima et al , 2002; Balasubramanian and Kuppuswamy, 2003; Gomez et al , 2010; Young et al , 2014; Hinz, 2015; O’Connor et al , 2015; Varney et al , 2016). Models of LINC complex ablation provide an opportunity to test whether communication of mechanical signals from the cytoskeleton to the nuclear interior (Lammerding et al , 2004; Lee et al , 2007; Hale et al , 2008; Stewart-Hutchinson et al , 2008; Luxton et al , 2010; Folker et al , 2011; Khatau et al , 2012; Long et al , 2013; Myat et al , 2015; Stewart et al , 2015) contributes to myocardium function, although to date this avenue of investigation has been largely unexplored.…”

Section: Introductionmentioning

confidence: 99%

Ablation of SUN2-containing LINC complexes drives cardiac hypertrophy without interstitial fibrosis

Stewart

Rodriguez

King

2019

MBoC

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The cardiomyocyte cytoskeleton, including the sarcomeric contractile apparatus, forms a cohesive network with cellular adhesions at the plasma membrane and nuclear–cytoskeletal linkages (LINC complexes) at the nuclear envelope. Human cardiomyopathies are genetically linked to the LINC complex and A-type lamins, but a full understanding of disease etiology in these patients is lacking. Here we show that SUN2-null mice display cardiac hypertrophy coincident with enhanced AKT/MAPK signaling, as has been described previously for mice lacking A-type lamins. Surprisingly, in contrast to lamin A/C-null mice, SUN2-null mice fail to show coincident fibrosis or upregulation of pathological hypertrophy markers. Thus, cardiac hypertrophy is uncoupled from profibrotic signaling in this mouse model, which we tie to a requirement for the LINC complex in productive TGFβ signaling. In the absence of SUN2, we detect elevated levels of the integral inner nuclear membrane protein MAN1, an established negative regulator of TGFβ signaling, at the nuclear envelope. We suggest that A-type lamins and SUN2 play antagonistic roles in the modulation of profibrotic signaling through opposite effects on MAN1 levels at the nuclear lamina, suggesting a new perspective on disease etiology.

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Drosophila KASH-domain protein Klarsicht regulates microtubule stability and integrin receptor localization during collective cell migration

Cited by 10 publications

References 49 publications

Signal Transduction across the Nuclear Envelope: Role of the LINC Complex in Bidirectional Signaling

Signal Transduction across the Nuclear Envelope: Role of the LINC Complex in Bidirectional Signaling

Microtubule Motors in Establishment of Epithelial Cell Polarity

Ablation of SUN2-containing LINC complexes drives cardiac hypertrophy without interstitial fibrosis

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