Moving and positioning the nucleus in skeletal muscle – one step at a time

Cadot, Bruno; Gache, Vincent; Gomes, Edgar R.

doi:10.1080/19491034.2015.1090073

Cited by 117 publications

(103 citation statements)

References 125 publications

(126 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Here, we examine nuclear positioning in the development of mammalian skeletal muscle as an example. Throughout mammalian muscle development, nuclei undergo at least five mechanistically and temporally distinct nuclear movements, making them an excellent system to study various mechanisms of nuclear migration in syncytia (Cadot et al, 2015). In mammalian skeletal muscle, A transmembrane actin-associated nuclear (TAN) line connects the retrogrademoving actin filaments to the nucleoskeleton.…”

Section: Nuclear Movements and Muscle Developmentmentioning

confidence: 99%

Nuclear migration events throughout development

Bone

Starr

2016

Journal of Cell Science

110

113

View full text Add to dashboard Cite

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.

show abstract

Section: Nuclear Movements and Muscle Developmentmentioning

confidence: 99%

Nuclear migration events throughout development

Bone

Starr

2016

Journal of Cell Science

110

113

View full text Add to dashboard Cite

show abstract

“…The binding of SUN-domain proteins to nesprins is required for maintaining the size of the lumen between the INM and the ONM (40, 285). This interaction is also required nuclear positioning in myofibers (29, 36, 96, 157). …”

Section: Nuclear Envelope Protein Functionmentioning

confidence: 99%

Diseases of the Nucleoskeleton

Holaska

2016

Comprehensive Physiology

View full text Add to dashboard Cite

The nucleus is separated from the cytosol by the nuclear envelope, which is a double lipid bilayer composed of the outer nuclear membrane and the inner nuclear membrane. The intermediate filament proteins lamin A, lamin B, and lamin C form a network underlying the inner nuclear membrane. This proteinaceous network provides the nucleus with its strength, rigidity, and elasticity. Positioned within the inner nuclear membrane are more than 150 inner nuclear membrane proteins, many of which interact directly with lamins and require lamins for their inner nuclear membrane localization. Inner nuclear membrane proteins and the nuclear lamins define the nuclear lamina. These inner nuclear membrane proteins have tissue-specific expression and diverse functions including regulating cytoskeletal organization, nuclear architecture, cell cycle dynamics, and genomic organization. Loss or mutations in lamins and inner nuclear membrane proteins cause a wide spectrum of diseases. Here, I will review the functions of the well-studied nuclear lamina proteins and the diseases associated with loss or mutations in these proteins. © 2016 American Physiological Society.

show abstract

“…Tissue powder was homogenized in RIPA buffer (SigmaAldrich) with the addition of protease inhibitors (cOmplete ULTRA Mini amphiphysin 2, but were unable to detect any changes in protein levels in the Klhl31-KO mice. However, proteomics did detect significant changes in nuclear membrane proteins, microtubuleassociated proteins, and Kif5b (Supplemental Table 1), all of which have been implicated in myonuclear positioning (49)(50)(51). Future studies will determine whether Klhl31 plays a direct role in the microtubule dynamics required for normal positioning of myonuclei.…”

Section: Generation Of Ska-slmap Transgenic Micementioning

confidence: 99%