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Molecular genetic analysis of muscle development, structure, and function in Drosophila.
In this chapter we discuss the ultrastructural and physiological properties of the diverse muscle types of Drosophila melanogaster and how genetic studies permit an understanding of muscle cell… Expand
Myosin heavy chain isoforms regulate muscle function but not myofibril assembly.
Data show that the proper MHC isoform is critical for specialized muscle function and myofibril stability, and introduced a gene encoding only an embryonic MHC into Drosophila melanogaster with unexpected results. Expand
Assembly of thick filaments and myofibrils occurs in the absence of the myosin head
Thick filament assembly and many aspects of myofibrillogenesis are independent of the myosin head and these processes are regulated by theMyosin rod and tailpiece, however, interaction of the the myOSin head with other myOfibrillar components is necessary for defining filament length and my ofibril dimensions. Expand
Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities
The first ultrastrutural characterization of a completely MHC- null muscle is presented and it is suggested that the differential sensitivity of muscle function to the Mhc1 mutation is a consequence of the unique myofilament arrays in each of these muscles. Expand
Vinculin network–mediated cytoskeletal remodeling regulates contractile function in the aging heart
- G. Kaushik, Alice Spenlehauer, +14 authors A. Engler
- Biology, Medicine
- Science Translational Medicine
- 17 June 2015
The findings suggest that the heart has molecular mechanisms to sustain performance and promote longevity, which may be assisted by therapeutic intervention to ameliorate the decline of function in aging patient hearts. Expand
Specific Myosin Heavy Chain Mutations Suppress Troponin I Defects in Drosophila Muscles
- W. A. Kronert, A. Acebes, A. Ferrús, S. Bernstein
- Biology, Medicine
- The Journal of cell biology
- 8 March 1999
It is concluded that the specific residues identified in myosin are important in regulating thick and thin filament interactions, and therefore could have implications for understanding gene interactions in human disease. Expand
X-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.
The first X-ray crystal structure of a UCS domain-containing protein, the UNC-45 myosin chaperone from Drosophila melanogaster, is reported, revealing that the central and UCS domains form a contiguous arrangement of 17 consecutive helical layers that arrange themselves into five discrete armadillo repeat subdomains. Expand
Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head.
There are four alternative regions that contribute to the motor domain of Drosophila myosin that are clustered at the distal end of the molecule, surrounding the reactive cysteine SH1 and the pivot point about which the light chain-containing region swings. Expand
Muscle‐specific accumulation of Drosophila myosin heavy chains: a splicing mutation in an alternative exon results in an isoform substitution.
- W. Kronert, K. Edwards, E. S. Roche, L. Wells, S. Bernstein
- Biology, Medicine
- The EMBO journal
- 1 September 1991
Analysis of this Drosophila muscle myosin heavy chain gene mutant illustrates that indirect flight muscles and jump muscles utilize different mechanisms for alternative RNA splicing. Expand
Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis
This is the first study of myosin isoform localization during insect embryogenesis, and forms the basis for transgenic and biochemical experiments designed to determine how MHC domains regulate muscle physiology. Expand