Visualization of cardiac ventricular myosin heavy chain homodimers and heterodimers by monoclonal antibody epitope mapping.

Dechesne, Claude J.; Bouvagnet, Patrice; Walzthöny, D; Leger, Jocelyne

doi:10.1083/jcb.105.6.3031

Cited by 45 publications

(37 citation statements)

References 34 publications

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“…Therefore, the dominant negative effect observed in these mutant cells is associated with the presence of singleheaded myosin II Although nothing is known about the mechanisms of coiledcoil formation in vivo, it is likely that the dimerization of two MHC peptides occurs post-translationally. This hypothesis is supported by the presence of myosin heterodimeric molecules in rat cardiac tissue and smooth muscle (19,20). Our results also support this hypothesis since we find heterodimeric singleheaded myosin molecules.…”

Section: Discussionsupporting

confidence: 81%

Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.

Burns

Larochelle

Erickson

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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Conventional myosin II is an essential protein for cytokinesis, capping of cell surface receptors, and development of Dictyostelium cells. Myosin II also plays an important role in the polarization and movement of cells. All conventional myosins are double-headed molecules but the significance of this structure is not understood since singleheaded myosin II can produce movement and force in vitro. We found that expression of the tail portion of myosin II in Dictyostelium led to the formation of single-headed myosin II in vivo. The resultant cells contain an approximately equal ratio of double-and single-headed myosin II molecules. Surprisingly, these cells were completely blocked in cytokinesis and capping of concanavalin A receptors although development into fruiting bodies was not impaired. We found that this phenotype is not due to defects in myosin light chain phosphorylation. These results show that single-headed myosin II cannot function properly in vivo and that it acts as a dominant negative mutation for myosin II function. These results suggest the possibility that cooperativity of myosin II heads is critical for force production in vivo.

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Section: Discussionsupporting

confidence: 81%

Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.

Burns

Larochelle

Erickson

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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“…This failure to trigger a change in the molecular regulation of other contractile protein genes is similar to the lack of response elicited from overexpression of the skeletal Tn-C isoform in the heart (36). Interestingly, overexpression of the wild type ␣-MHC exhibits limited, if any, cardiac abnormalities, 3 a result similar to our findings with the ␣-MHC/␤-TM transgenic mice. Thus, it appears that overexpression of contractile protein genes in vertebrates may lead to physiological changes in cardiac function, 3 L. Leinwand, personal communication.…”

Section: Figsupporting

confidence: 79%

Molecular and Physiological Effects of Overexpressing Striated Muscle β-Tropomyosin in the Adult Murine Heart

Muthuchamy

Grupp

et al. 1995

Journal of Biological Chemistry

144

161

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Tropomyosins comprise a family of actin-binding proteins that are central to the control of calcium-regulated striated muscle contraction. To understand the functional role of tropomyosin isoform differences in cardiac muscle, we generated transgenic mice that overexpress striated muscle-specific ␤-tropomyosin in the adult heart. Nine transgenic lines show a 150-fold increase in ␤-tropomyosin mRNA expression in the heart, along with a 34-fold increase in the associated protein. This increase in ␤-tropomyosin message and protein causes a concomitant decrease in the level of ␣-tropomyosin transcripts and their associated protein. There is a preferential formation of the ␣␤-heterodimer in the transgenic mouse myofibrils, and there are no detectable alterations in the expression of other contractile protein genes, including the endogenous ␤-tropomyosin isoform. When expression from the ␤-tropomyosin transgene is terminated, ␣-tropomyosin expression returns to normal levels. No structural changes were observed in these transgenic hearts nor in the associated sarcomeres. Interestingly, physiological analyses of these hearts using a work-performing model reveal a significant effect on diastolic function. As such, this study demonstrates that a coordinate regulatory mechanism exists between ␣-and ␤-tropomyosin gene expression in the murine heart, which results in a functional correlation between ␣-and ␤-tropomyosin isoform content and cardiac performance.

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“…Significant motility of eGFP-myosin fusions was also shown previously (Reisen and Hanson, 2007;Sparkes et al, 2008). Heterodimers of myosins were detected in low percentage in different systems; however, it was shown that homodimers are more thermodynamically stable (Dechesne et al, 1987;Kerwin and Bandman, 1991;Singh and Bandman, 2006), and heterodimerization of plant myosins is still to be tested. Interestingly, heterologous interaction between two subdomains of the globular tails GT1 from MYA1 and GT2 from MYA2, XI-C, or XI-K was observed in yeast two-hybrid analysis (Li and Nebenfü hr, 2007).…”

Section: Discussionmentioning

confidence: 88%

A Comparative Study of the Involvement of 17 Arabidopsis Myosin Family Members on the Motility of Golgi and Other Organelles

et al. 2009

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Gene families with multiple members are predicted to have individuals with overlapping functions. We examined all of the Arabidopsis (Arabidopsis thaliana) myosin family members for their involvement in Golgi and other organelle motility. Truncated fragments of all 17 annotated Arabidopsis myosins containing either the IQ tail or tail domains only were fused to fluorescent markers and coexpressed with a Golgi marker in two different plants. We tracked and calculated Golgi body displacement rate in the presence of all myosin truncations and found that tail fragments of myosins MYA1, MYA2, XI-C, XI-E, XI-I, and XI-K were the best inhibitors of Golgi body movement in the two plants. Tail fragments of myosins XI-B, XI-F, XI-H, and ATM1 had an inhibitory effect on Golgi bodies only in Nicotiana tabacum, while tail fragments of myosins XI-G and ATM2 had a slight effect on Golgi body motility only in Nicotiana benthamiana. The best myosin inhibitors of Golgi body motility were able to arrest mitochondrial movement too. No exclusive colocalization was found between these myosins and Golgi bodies in our system, although the excess of cytosolic signal observed could mask myosin molecules bound to the surface of the organelle. From the preserved actin filaments found in the presence of enhanced green fluorescent protein fusions of truncated myosins and the motility of myosin punctae, we conclude that global arrest of actomyosin-derived cytoplasmic streaming had not occurred. Taken together, our data suggest that the above myosins are involved, directly or indirectly, in the movement of Golgi and mitochondria in plant cells.The Arabidopsis (Arabidopsis thaliana) myosin gene family contains 17 members: myosin group XI, which includes 13 members (myosins XI-

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Visualization of cardiac ventricular myosin heavy chain homodimers and heterodimers by monoclonal antibody epitope mapping.

Cited by 45 publications

References 34 publications

Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.

Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.

Molecular and Physiological Effects of Overexpressing Striated Muscle β-Tropomyosin in the Adult Murine Heart

A Comparative Study of the Involvement of 17 Arabidopsis Myosin Family Members on the Motility of Golgi and Other Organelles

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