Samp1 is a component of TAN lines and is required for nuclear movement

Borrego-Pinto, Joana; Jegou, Thibaud; Osório, Daniel S.; Aurade, Frédéric; Gorjánácz, Mátyás; Koch, Birgit; Mattaj, Iain W.; Gomes, Edgar R.

doi:10.1242/jcs.087049

Cited by 96 publications

(102 citation statements)

References 23 publications

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“…Sun-2 and Nesprin-2 giant are essential components of these TAN lines, which associate with dorsal actin cables at the cytoplasmic surface of the nucleus and are anchored via lamins to the nuclear interior. The INM proteins Samp and emerin (Borrego-Pinto et al 2012;Chang et al 2013) were also found in these complexes. TAN lines at the nuclear membrane resemble in many aspects FA complexes at the plasma membrane.…”

Section: The Route and Components Of Mechanosensingmentioning

confidence: 95%

Lamins at the crossroads of mechanosignaling

2015

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The intermediate filament proteins, A-and B-type lamins, form the nuclear lamina scaffold adjacent to the inner nuclear membrane. B-type lamins confer elasticity, while A-type lamins lend viscosity and stiffness to nuclei. Lamins also contribute to chromatin regulation and various signaling pathways affecting gene expression. The mechanical roles of lamins and their functions in gene regulation are often viewed as independent activities, but recent findings suggest a highly cross-linked and interdependent regulation of these different functions, particularly in mechanosignaling. In this newly emerging concept, lamins act as a ''mechanostat'' that senses forces from outside and responds to tension by reinforcing the cytoskeleton and the extracellular matrix. A-type lamins, emerin, and the linker of the nucleoskeleton and cytoskeleton (LINC) complex directly transmit forces from the extracellular matrix into the nucleus. These mechanical forces lead to changes in the molecular structure, modification, and assembly state of A-type lamins. This in turn activates a tension-induced ''inside-out signaling'' through which the nucleus feeds back to the cytoskeleton and the extracellular matrix to balance outside and inside forces. These functions regulate differentiation and may be impaired in lamin-linked diseases, leading to cellular phenotypes, particularly in mechanical load-bearing tissues.

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Section: The Route and Components Of Mechanosensingmentioning

confidence: 95%

Lamins at the crossroads of mechanosignaling

2015

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“…S2). As nesprin-2G has been shown to colocalize with actin fibers in the perinuclear region and to regulate nuclear motion (Borrego-Pinto et al, 2012;Luxton et al, 2010), the depletion of this LINC protein significantly reduced the fraction of cells that formed an actin cap (supplementary material Fig. S2A,B).…”

Section: The Actin Cap Controls Cell Migrationmentioning

confidence: 98%

Tight coupling between nucleus and cell migration through the perinuclear actin cap

Kim¹,

Cho²,

Wirtz³

2014

Journal of Cell Science

108

125

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Although eukaryotic cells are known to alternate between 'advancing' episodes of fast and persistent movement and 'hesitation' episodes of low speed and low persistence, the molecular mechanism that controls the dynamic changes in morphology, speed and persistence of eukaryotic migratory cells remains unclear. Here, we show that the movement of the interphase nucleus during random cell migration switches intermittently between two distinct modes -rotation and translocation -that follow with high fidelity the sequential rounded and elongated morphologies of the nucleus and cell body, respectively. Nuclear rotation and translocation mediate the stopand-go motion of the cell through the dynamic formation and dissolution, respectively, of the contractile perinuclear actin cap, which is dynamically coupled to the nuclear lamina and the nuclear envelope through LINC complexes. A persistent cell movement and nuclear translocation driven by the actin cap are halted following the disruption of the actin cap, which in turn allows the cell to repolarize for its next persistent move owing to nuclear rotation mediated by cytoplasmic dynein light intermediate chain 2.

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“…Although mutations in lamin A or emerin result in non-moving nuclei, TAN lines still glide along the surface of the nuclear envelope (Chang et al, 2013a;Folker et al, 2011). The inner nuclear membrane protein spindle-associated membrane protein 1 (Samp1; also known as NET5 and officially known as TMEM201) is an additional component of TAN lines and functions, in part, to connect Sun2 to lamin A (Borrego-Pinto et al, 2012). On the cytoplasmic side of TAN lines, the formin FHOD1 plays a structural role.…”

Section: Nuclear Migration In Polarizing Adherent Tissue Culture Cellsmentioning

confidence: 99%

Nuclear migration events throughout development

Bone

Starr

2016

Journal of Cell Science

103

113

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Moving the nucleus to a specific position within the cell is an important event during many cell and developmental processes. Several different molecular mechanisms exist to position nuclei in various cell types. In this Commentary, we review the recent progress made in elucidating mechanisms of nuclear migration in a variety of important developmental models. Genetic approaches to identify mutations that disrupt nuclear migration in yeast, filamentous fungi, Caenorhabditis elegans, Drosophila melanogaster and plants led to the identification of microtubule motors, as well as Sad1p, UNC-84 (SUN) domain and Klarsicht, ANC-1, Syne homology (KASH) domain proteins (LINC complex) that function to connect nuclei to the cytoskeleton. We focus on how these proteins and various mechanisms move nuclei during vertebrate development, including processes related to wound healing of fibroblasts, fertilization, developing myotubes and the developing central nervous system. We also describe how nuclear migration is involved in cells that migrate through constricted spaces. On the basis of these findings, it is becoming increasingly clear that defects in nuclear positioning are associated with human diseases, syndromes and disorders.

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Samp1 is a component of TAN lines and is required for nuclear movement

Cited by 96 publications

References 23 publications

Lamins at the crossroads of mechanosignaling

Lamins at the crossroads of mechanosignaling

Tight coupling between nucleus and cell migration through the perinuclear actin cap

Nuclear migration events throughout development

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