Molecular Genetic Analysis of Muscle Development, Structure, and Function in Drosophila

Bernstein, Sanford I.; O'Donnell, Patrick T.; Cripps, Richard M.

doi:10.1016/s0074-7696(08)61874-4

Cited by 164 publications

(142 citation statements)

References 244 publications

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“…Emb myosin is normally expressed in the supercontractile dorsal oblique muscles that have long sarcomeres and a high degree of shortening (49). The mechanical properties of these muscles are unknown, but they are used to power crawling at 1 mm⅐s Ϫ1 , 2 with individual contractions visible to the naked eye, and must have much slower contraction velocities than IFMs.…”

Section: Discussionmentioning

confidence: 99%

Alternative Exon-encoded Regions of Drosophila Myosin Heavy Chain Modulate ATPase Rates and Actin Sliding Velocity

Swank¹,

Bartoo

Knowles

et al. 2001

Journal of Biological Chemistry

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137

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To investigate the molecular functions of the regions encoded by alternative exons from the single Drosophila myosin heavy chain gene, we made the first kinetic measurements of two muscle myosin isoforms that differ in all alternative regions. Myosin was purified from the indirect flight muscles of wild-type and transgenic flies expressing a major embryonic isoform. The in vitro actin sliding velocity on the flight muscle isoform (6.4 m⅐s ؊1 at 22°C) is among the fastest reported for a type II myosin and was 9-fold faster than with the embryonic isoform. With smooth muscle tropomyosin bound to actin, the actin sliding velocity on the embryonic isoform increased 6-fold, whereas that on the flight muscle myosin slightly decreased. No difference in the step sizes of Drosophila and rabbit skeletal myosins were found using optical tweezers, suggesting that the slower in vitro velocity with the embryonic isoform is due to altered kinetics. Basal ATPase rates for flight muscle myosin are higher than those of embryonic and rabbit myosin. These differences explain why the embryonic myosin cannot functionally substitute in vivo for the native flight muscle isoform, and demonstrate that one or more of the five myosin heavy chain alternative exons must influence Drosophila myosin kinetics.

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Section: Discussionmentioning

confidence: 99%

Alternative Exon-encoded Regions of Drosophila Myosin Heavy Chain Modulate ATPase Rates and Actin Sliding Velocity

Swank¹,

Bartoo

Knowles

et al. 2001

Journal of Biological Chemistry

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137

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“…This subject has been reviewed by Bernstein et al (1993) and more recent studies on the molecular biology of contractile proteins have been reported (Barbas et al, 1993;Cripps et al, 1994;Kronert et al, 1994Kronert et al, , 1995Vigoreaux, 1994).…”

Section: Introductionmentioning

confidence: 99%

Flight muscle function in Drosophila requires colocalization of glycolytic enzymes.

Wojtas

Slepecky

Kalm

et al. 1997

MBoC

111

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Structural relationships between the myofibrillar contractile apparatus and the enzymes that generate ATP for muscle contraction are not well understood. We explored whether glycolytic enzymes are localized in Drosophila flight muscle and whether localization is required for function. We find that glycerol-3-phosphate dehydrogenase (GPDH) is localized at Z-discs and M-lines. The glycolytic enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are also localized along the sarcomere with a periodic pattern that is indistinguishable from that of GPDH localization. Furthermore, localization of aldolase and GAPDH requires simultaneous localization of GPDH, because aldolase and GAPDH are not localized along the sarcomere in muscles of strains that carry Gpdh null alleles. In an attempt to understand the process of glycolytic enzyme colocalization, we have explored in more detail the mechanism of GPDH localization. In flight muscle, there is only one GPDH isoform, GPDH-1, which is distinguished from isoforms found in other tissues by having three C-terminal amino acids: glutamine, asparagine, and leucine. Transgenic flies that can produce only GPDH-1 display enzyme colocalization similar to wild-type flies. However, transgenic flies that synthesize only GPDH-3, lacking the C-terminal tripeptide, do not show the periodic banding pattern of localization at Z-discs and M-lines for GPDH. In addition, neither GAPDH nor aldolase colocalize at Z-discs and M-lines in the sarcomeres of muscles from GPDH-3 transgenic flies. Failure of the glycolytic enzymes to colocalize in the sarcomere results in the inability to fly, even though the full complement of active glycolytic enzymes is present in flight muscles. Therefore, the presence of active enzymes in the cell is not sufficient for muscle function; colocalization of the enzymes is required. These results indicate that the mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly organized cellular system.

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“…Drosophila's thin filaments contain homologues of the proteins found in vertebrate muscle. Actin, a-actinin, tropomyosin, TnT, TnI, and TnC have all been identified and sequenced (see Bernstein et al, 1993 for a review). In addition, insect muscles contain peculiar myofibrillar proteins such as arthrin and troponin H. In view of the large diversity of TnI isoforms and their muscle-specific expression pattern (Barbas et al, 1993) it seems plausible that this protein(s) plays distinct functional roles that the in vitro studies carried out so far cannot discriminate.…”

Section: Introductionmentioning

confidence: 99%

Functional recovery of troponin I in a Drosophila heldup mutant after a second site mutation.

Prado

Canal

Barbas

et al. 1995

MBoC

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To identify proteins that interact in vivo with muscle components we have used a genetic approach based on the isolation of suppressors of mutant alleles of known muscle components. We have applied this system to the case of troponin I (TnI) in Drosophila and its mutant allele heldup2 (hdp2). This mutation causes an alanine to valine substitution at position 116 after a single nucleotide change in a constitutive exon. Among the isolated suppressors, one of them results from a second site mutation at the TnI gene itself. Muscles endowed with TnI mutated at both sites support nearly normal myofibrillar structure, perform notably well in wing beating and flight tests, and isolated muscle fibers produce active force. We show that the structural and functional recovery in this suppressor does not result from a change in the stoichiometric ratio of TnI isoforms. The second site suppression is due to a leucine to phenylalanine change within a heptameric leucine string motif adjacent to the actin binding domain of TnI. These data evidence a structural and functional role for the heptameric leucine string that is most noticeable, if not specific, in the indirect flight muscle. INTRODUCTIONThe regulation of contraction in striated muscle occurs by mechanisms that are remarkably similar throughout the animal kingdom. Nerve input results in the

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Molecular Genetic Analysis of Muscle Development, Structure, and Function in Drosophila

Cited by 164 publications

References 244 publications

Alternative Exon-encoded Regions of Drosophila Myosin Heavy Chain Modulate ATPase Rates and Actin Sliding Velocity

Alternative Exon-encoded Regions of Drosophila Myosin Heavy Chain Modulate ATPase Rates and Actin Sliding Velocity

Flight muscle function in Drosophila requires colocalization of glycolytic enzymes.

Functional recovery of troponin I in a Drosophila heldup mutant after a second site mutation.

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