scholarly journals A novel isoform of MAP4 organises the paraxial microtubule array required for muscle cell differentiation

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Binyam Mogessie ◽  
Daniel Roth ◽  
Zainab Rahil ◽  
Anne Straube
Keyword(s):  
Cell Differentiation ◽  
Cell Fusion ◽  
Muscle Cell ◽  
Cell Elongation ◽  
Myogenic Differentiation ◽  
Muscle Cells ◽  
Microtubule Array ◽  
Muscle Cell Differentiation ◽  
Microtubule Transport

The microtubule cytoskeleton is critical for muscle cell differentiation and undergoes reorganisation into an array of paraxial microtubules, which serves as template for contractile sarcomere formation. In this study, we identify a previously uncharacterised isoform of microtubule-associated protein MAP4, oMAP4, as a microtubule organising factor that is crucial for myogenesis. We show that oMAP4 is expressed upon muscle cell differentiation and is the only MAP4 isoform essential for normal progression of the myogenic differentiation programme. Depletion of oMAP4 impairs cell elongation and cell–cell fusion. Most notably, oMAP4 is required for paraxial microtubule organisation in muscle cells and prevents dynein- and kinesin-driven microtubule–microtubule sliding. Purified oMAP4 aligns dynamic microtubules into antiparallel bundles that withstand motor forces in vitro. We propose a model in which the cooperation of dynein-mediated microtubule transport and oMAP4-mediated zippering of microtubules drives formation of a paraxial microtubule array that provides critical support for the polarisation and elongation of myotubes.

The neural tube/notochord complex is necessary for vertebral but not limb and body wall striated muscle differentiation

Development ◽  
1992 ◽  
Vol 115 (3) ◽  
pp. 657-672 ◽  
Author(s):  
P.M. Rong ◽  
M.A. Teillet ◽  
C. Ziller ◽  
N.M. Le Douarin
Keyword(s):  
Cell Differentiation ◽  
Muscle Cell ◽  
Neural Tube ◽  
Body Wall ◽  
Muscle Cells ◽  
Avian Embryo ◽  
Muscle Cell Differentiation ◽  
Cell Commitment ◽  
Axial Organs

The aim of this work was to investigate the role played by the axial organs, neural tube and notochord, on the differentiation of muscle cells from the somites in the avian embryo. Two of us have previously shown that neuralectomy and notochordectomy is followed by necrosis of the somites and consecutive absence of vertebrae and of most muscle cells derived from the myotomes while the limbs develop normally with muscles. Here we have focused our attention on muscle cell differentiation by using the 13F4 mAb that recognizes a cytoplasmic antigen specific of all types of muscle cells. We show that differentiation of muscle cells of myotomes can occur in the absence of notochord and neural tube provided that the somites from which they are derived have been in contact with the axial organs for a defined period of time, about 10 hours for the first somites formed at the cervical level, a duration that progressively reduces caudalward (i.e. for thoracic and lumbar somites). Either one or the other of the two axial organs, the neural tube or the notochord can prevent somitic cell death and fulfill the requirements for myotomal muscle cell differentiation. Separation of the neural tube/notochord complex from the somites by a surgical slit on one side of the embryo gave the same results as extirpation of these organs and provided a perfect control on the non-operated side. A striking finding was that limb and body wall muscles, although derived from the somites, differentiated in the absence of the axial organs. However, limb muscles that develop after excision of the neural tube started to degenerate from E10 onward due to lack of innervation. In vitro explantation of somites from different axial levels confirmed and defined precisely the chronology of muscle cell commitment in the myotomes as revealed by the in vivo experiments.

scholarly journals Expression of rainbow trout glucose transporters GLUT1 and GLUT4 during in vitro muscle cell differentiation and regulation by insulin and IGF-I

2009 ◽  
Vol 296 (3) ◽  
pp. R794-R800 ◽  
Author(s):  
Mònica Díaz ◽  
Yoryia Vraskou ◽  
Joaquim Gutiérrez ◽  
Josep V. Planas
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Glucose Uptake ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Muscle Cell Differentiation ◽  
Igf I ◽  
Glut1 Expression ◽  
Trout Muscle

Insulin is an important factor for the maintenance of glucose homeostasis, enhancing glucose uptake in its target tissues in a process that has been conserved between fish and mammals. In fish skeletal muscle cells, like in mammals, insulin promotes GLUT4 translocation to the plasma membrane and, consequently, glucose uptake, but its role regulating the expression of glucose transporters in vitro has not been demonstrated to date. Thus, we investigated the expression of GLUT4 and GLUT1 throughout skeletal muscle cell differentiation and their regulation by insulin and IGF-I using a primary culture of trout muscle cells. GLUT4 expression gradually increased during the muscle cell differentiation process, whereas GLUT1 expression remained fairly constant. Insulin and IGF-I similarly increased the mRNA levels of GLUT4 in myoblasts and myotubes. On the other hand, IGF-I appeared to be more potent than insulin in stimulating GLUT1 expression, particularly at the myoblast stage. Therefore, this work provides the first demonstration in nonmammalian vertebrates that insulin and IGF-I may act directly on trout muscle cells to regulate the expression of GLUT4 and GLUT1.

scholarly journals Dual-specificity phosphatase 4 is upregulated during skeletal muscle atrophy and modulates extracellular signal-regulated kinase activity

2019 ◽  
Vol 316 (4) ◽  
pp. C567-C581 ◽  
Author(s):  
Ashley N. Haddock ◽  
Sydney A. Labuzan ◽  
Amy E. Haynes ◽  
Caleb S. Hayes ◽  
Karina M. Kakareka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Map Kinase ◽  
Reporter Gene ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Skeletal Muscle Atrophy ◽  
Kinase Signaling ◽  
Muscle Cell Differentiation ◽  
Map Kinase Signaling

Skeletal muscle atrophy results from disparate physiological conditions, including denervation, corticosteroid treatment, and aging. The purpose of this study was to describe and characterize the function of dual-specificity phosphatase 4 (Dusp4) in skeletal muscle after it was found to be induced in response to neurogenic atrophy. Quantitative PCR and Western blot analysis revealed that Dusp4 is expressed during myoblast proliferation but rapidly disappears as muscle cells differentiate. The Dusp4 regulatory region was cloned and found to contain a conserved E-box element that negatively regulates Dusp4 reporter gene activity in response to myogenic regulatory factor expression. In addition, the proximal 3′-untranslated region of Dusp4 acts in an inhibitory manner to repress reporter gene activity as muscle cells progress through the differentiation process. To determine potential function, Dusp4 was fused with green fluorescent protein, expressed in C2C12 cells, and found to localize to the nucleus of proliferating myoblasts. Furthermore, Dusp4 overexpression delayed C2C12 muscle cell differentiation and resulted in repression of a MAP kinase signaling pathway reporter gene. Ectopic expression of a Dusp4 dominant negative mutant blocked muscle cell differentiation and attenuated MAP kinase signaling by preferentially targeting the ERK1/2 branch, but not the p38 branch, of the MAP kinase signaling cascade in skeletal muscle cells. The findings presented in this study provide the first description of Dusp4 in skeletal muscle and suggest that Dusp4 may play an important role in the regulation of muscle cell differentiation by regulating MAP kinase signaling.

scholarly journals USP19 deubiquitinating enzyme inhibits muscle cell differentiation by suppressing unfolded-protein response signaling

2015 ◽  
Vol 26 (5) ◽  
pp. 913-923 ◽  
Author(s):  
Benjamin Wiles ◽  
Miao Miao ◽  
Erin Coyne ◽  
Louise Larose ◽  
Andrey V. Cybulsky ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Unfolded Protein Response ◽  
Muscle Cell ◽  
Deubiquitinating Enzyme ◽  
Muscle Cell Differentiation ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

USP19 deubiquitinating enzyme has two isoforms, cytoplasmic and endoplasmic reticulum (ER) localized. The ER-localized isoform specifically suppresses muscle cell differentiation in vitro and appears to do so by inhibiting the unfolded-protein response that occurs during such differentiation. In vivo, loss of USP19 promotes muscle regeneration following injury.

scholarly journals Smooth Muscle Cell Differentiation In Vitro

2011 ◽  
Vol 31 (7) ◽  
pp. 1485-1494 ◽  
Author(s):  
Changqing Xie ◽  
Raquel P. Ritchie ◽  
Huarong Huang ◽  
Jifeng Zhang ◽  
Y. Eugene Chen
Keyword(s):  
Smooth Muscle ◽  
Cell Differentiation ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Muscle Cell Differentiation ◽  
Smooth Muscle Cell Differentiation

scholarly journals Changes in the mechanism of Ca2+ mobilization during the differentiation of BC3H1 muscle cells

1991 ◽  
Vol 273 (1) ◽  
pp. 219-223 ◽  
Author(s):  
H De Smedt ◽  
J B Parys ◽  
B Himpens ◽  
L Missiaen ◽  
R Borghgraef
Keyword(s):  
Cell Differentiation ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Proliferating Cells ◽  
Muscle Cell Differentiation ◽  
Differentiated Cells

Ca2+ sequestration and release in BC3H1 muscle cells is strongly dependent on the stage of differentiation. In proliferating cells, more than 90% of the sequestered Ca2+ was Ins(1,4,5)P3-sensitive and 25% was caffeine-sensitive. In differentiated cells, the Ca2+ accumulation was 5-fold higher and was InsP3-insensitive, but about 60% of the sequestered Ca2+ was caffeine-sensitive. These changes were reversible upon addition of growth stimuli. Similarly, by measuring the intracellular Ca2+ concentration in single intact BC3H1 cells, it was found that the number of histamine-responsive cells decreased and the number of caffeine-responsive cells increased during muscle cell differentiation. These data indicate that the development of the muscle phenotype in BC3H1 myoblasts induces a major rearrangement of the mechanisms for Ca2+ mobilization.

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