Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle

Kulke M, Neagoe C, Kolmerer B, Minajeva A, Hinssen H, Bullard B, Linke WA (2001)
JOURNAL OF CELL BIOLOGY 154(5): 1045-1058.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
Kettin is a high molecular mass protein of insect muscle that in the sarcomeres binds to actin and a-actinin. To investigate kettin's functional role, we combined immunolabeling experiments with mechanical and biochemical studies on indirect flight muscle (IFM) myofibrils of Drosophila melanogaster. Micrographs of stretched IFM sarcomeres labeled with kettin antibodies revealed staining of the Z-disc periphery. After extraction of the kettin-associated actin, the A-band edges were also stained. In contrast, the staining pattern of projectin, another IFM-1-band protein, was not altered by actin removal. Force measurements were performed on single IFM myofibrils to establish the passive length-tension relationship and record passive stiffness. Stiffness decreased within seconds during gelsolin incubation and to a similar degree upon kettin digestion with mu -calpain. Immunoblotting demonstrated the presence of kettin isoforms in normal Drosophila IFM myofibrils and in myofibrils from an actin-null mutant. Dotblot analysis revealed binding of COOH-terminal kettin domains to myosin. We conclude that kettin is attached not only to actin but also to the end of the thick filament. Kettin along with projectin may constitute the elastic filament system of insect IFM and determine the muscle's high stiffness necessary for stretch activation. Possibly, the two proteins modulate myofibrillar stiffness by expressing different size isoforms.
Publishing Year
ISSN
PUB-ID

Cite this

Kulke M, Neagoe C, Kolmerer B, et al. Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle. JOURNAL OF CELL BIOLOGY. 2001;154(5):1045-1058.
Kulke, M., Neagoe, C., Kolmerer, B., Minajeva, A., Hinssen, H., Bullard, B., & Linke, W. A. (2001). Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle. JOURNAL OF CELL BIOLOGY, 154(5), 1045-1058.
Kulke, M., Neagoe, C., Kolmerer, B., Minajeva, A., Hinssen, H., Bullard, B., and Linke, W. A. (2001). Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle. JOURNAL OF CELL BIOLOGY 154, 1045-1058.
Kulke, M., et al., 2001. Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle. JOURNAL OF CELL BIOLOGY, 154(5), p 1045-1058.
M. Kulke, et al., “Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle”, JOURNAL OF CELL BIOLOGY, vol. 154, 2001, pp. 1045-1058.
Kulke, M., Neagoe, C., Kolmerer, B., Minajeva, A., Hinssen, H., Bullard, B., Linke, W.A.: Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle. JOURNAL OF CELL BIOLOGY. 154, 1045-1058 (2001).
Kulke, M, Neagoe, C, Kolmerer, B, Minajeva, A, Hinssen, Horst, Bullard, B, and Linke, WA. “Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle”. JOURNAL OF CELL BIOLOGY 154.5 (2001): 1045-1058.
This data publication is cited in the following publications:
This publication cites the following data publications:

36 Citations in Europe PMC

Data provided by Europe PubMed Central.

Elastic proteins in the flight muscle of Manduca sexta.
Yuan CC, Ma W, Schemmel P, Cheng YS, Liu J, Tsaprailis G, Feldman S, Ayme Southgate A, Irving TC., Arch. Biochem. Biophys. 568(), 2015
PMID: 25602701
Distinct genetic programs guide Drosophila circular and longitudinal visceral myoblast fusion.
Rudolf A, Buttgereit D, Jacobs M, Wolfstetter G, Kesper D, Putz M, Berger S, Renkawitz-Pohl R, Holz A, Onel SF., BMC Cell Biol. 15(), 2014
PMID: 25000973
An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight.
Wang Q, Newhard CS, Ramanath S, Sheppard D, Swank DM., J. Exp. Biol. 217(Pt 2), 2014
PMID: 24115062
Molecular analysis of the muscle protein projectin in Lepidoptera.
Ayme-Southgate AJ, Turner L, Southgate RJ., J. Insect Sci. 13(), 2013
PMID: 24206568
Mutations in Drosophila myosin rod cause defects in myofibril assembly.
Salvi SS, Kumar RP, Ramachandra NB, Sparrow JC, Nongthomba U., J. Mol. Biol. 419(1-2), 2012
PMID: 22370558
Deletion of Drosophila muscle LIM protein decreases flight muscle stiffness and power generation.
Clark KA, Lesage-Horton H, Zhao C, Beckerle MC, Swank DM., Am. J. Physiol., Cell Physiol. 301(2), 2011
PMID: 21562304
Projectin PEVK domain, splicing variants and domain structure in basal and derived insects.
Ayme-Southgate A, Philipp RA, Southgate RJ., Insect Mol. Biol. 20(3), 2011
PMID: 21349121
Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.
Miller MS, Tanner BC, Nyland LR, Vigoreaux JO., J. Biomed. Biotechnol. 2010(), 2010
PMID: 20625489
Molecular and biochemical characterization of kettin in Caenorhabditis elegans.
Ono S, Mohri K, Ono K., J. Muscle Res. Cell. Motil. 26(6-8), 2005
PMID: 16453162
Passive stiffness of Drosophila IFM myofibrils: a novel, high accuracy measurement method.
Hao Y, Bernstein SI, Pollack GH., J. Muscle Res. Cell. Motil. 25(4-5), 2004
PMID: 15548865

51 References

Data provided by Europe PubMed Central.

Drosophila D-titin is required for myoblast fusion and skeletal muscle striation.
Zhang Y, Featherstone D, Davis W, Rushton E, Broadie K., J. Cell. Sci. 113 ( Pt 17)(), 2000
PMID: 10934048

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 11535621
PubMed | Europe PMC

Search this title in

Google Scholar