Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans 1 1Edited by J. Karn

Kolmerer, Bernhard; Clayton, Jonathan D.; Beneš, Vladimír; Allen, Taylor; Ferguson, Charles; Leonard, Kevin; Weber, Ursula; Knekt, Marika; Ansorge, Wilhelm; Labeit, Siegfried; Bullard, Belinda

doi:10.1006/jmbi.1999.3461

Cited by 43 publications

(52 citation statements)

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“…Kettin is one of the first proteins to colocalize with actin during the early stages of myofibrillogenesis (Ayme-Southgate et al, 2004), and genetic analysis has shown that it is essential for myofibril assembly in the fruit fly (Hakeda et al, 2000). The sequence of kettin contains 35 immunoglobulin-like (Ig) repeats separated by short linker sequences (Hakeda et al, 2000;Kolmerer et al, 2000) and is related to the connectin/titin family of giant elastic proteins (Maruyama, 1997;Gautel et al, 1999;Gregorio et al, 1999;Maruyama and Kimura, 2000;Granzier et al, 2002). However, kettin does not have fibronectin-like, elastic PEVK, or kinase domains, and seems to be a uniquely evolved member of the connectin/titin family of proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Based on sequence homology, a gene coding for a kettinlike protein has been found in the nematode Caenorhabditis elegans (Hakeda et al, 2000;Kolmerer et al, 2000). Transcripts of this gene are expressed in various muscle cells, and a Abbreviations used: GST, glutathione S-transferase; Ig, immunoglobulin-like; RNAi, RNA interference.…”

Section: Introductionmentioning

confidence: 99%

“…Based on sequence homology, a gene coding for a kettinlike protein has been found in the nematode Caenorhabditis elegans (Hakeda et al, 2000;Kolmerer et al, 2000). Transcripts of this gene are expressed in various muscle cells, and a monoclonal antibody (mAb) against insect kettin reacts with the dense bodies in obliquely striated body wall muscle (Kolmerer et al, 2000), which is equivalent to the Z-lines in cross-striated muscle.…”

Section: Introductionmentioning

confidence: 99%

“…Importantly, recent molecular genetic studies have shown that kettin is a splice variant of connectin/titin in Drosophila (Machado and Andrew, 2000;Zhang et al, 2000) and crayfish (Fukuzawa et al, 2001). Therefore, the previously reported phenotype of the Drosophila kettin mutants (Hakeda et al, 2000) may be partly due to a defect in the D-titin gene.Based on sequence homology, a gene coding for a kettinlike protein has been found in the nematode Caenorhabditis elegans (Hakeda et al, 2000;Kolmerer et al, 2000). Transcripts of this gene are expressed in various muscle cells, and a Abbreviations used: GST, glutathione S-transferase; Ig, immunoglobulin-like; RNAi, RNA interference.…”

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confidence: 99%

“…© 2006 by The American Society for Cell Biology monoclonal antibody (mAb) against insect kettin reacts with the dense bodies in obliquely striated body wall muscle (Kolmerer et al, 2000), which is equivalent to the Z-lines in cross-striated muscle. However, the product of the C. elegans kettin-like gene has not been extensively studied at the protein level.…”

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Caenorhabditis elegansKettin, a Large Immunoglobulin-like Repeat Protein, Binds to Filamentous Actin and Provides Mechanical Stability to the Contractile Apparatuses in Body Wall Muscle

Ono

Mohri

et al. 2006

MBoC

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Kettin is a large actin-binding protein with immunoglobulin-like (Ig) repeats, which is associated with the thin filaments in arthropod muscles. Here, we report identification and functional characterization of kettin in the nematode Caenorhabditis elegans. We found that one of the monoclonal antibodies that were raised against C. elegans muscle proteins specifically reacts with kettin (Ce-kettin). We determined the entire cDNA sequence of Ce-kettin that encodes a protein of 472 kDa with 31 Ig repeats. Arthropod kettins are splice variants of much larger connectin/titin-related proteins. However, the gene for Ce-kettin is independent of other connectin/titin-related genes. Ce-kettin localizes to the thin filaments near the dense bodies in both striated and nonstriated muscles. The C-terminal four Ig repeats and the adjacent non-Ig region synergistically bind to actin filaments in vitro. RNA interference of Ce-kettin caused weak disorganization of the actin filaments in body wall muscle. This phenotype was suppressed by inhibiting muscle contraction by a myosin mutation, but it was enhanced by tetramisole-induced hypercontraction. Furthermore, Ce-kettin was involved in organizing the cytoplasmic portion of the dense bodies in cooperation with ␣-actinin. These results suggest that kettin is an important regulator of myofibrillar organization and provides mechanical stability to the myofibrils during contraction. INTRODUCTIONIn muscle cells, the actin cytoskeleton is highly differentiated to form the myofibrils that are specialized for producing contractile forces. In addition to actin and myosin as the essential contractile components, regulatory components for the contractile activity are integrated into the structure (Squire, 1997). Despite the fact that many myofibrillar components have been identified, little is known about how these components functionally interact to assemble and maintain the myofibrils in living cells (Littlefield and Fowler, 1998;Gregorio and Antin, 2000;Clark et al., 2002). In particular, the assembly process of actin filaments is complex. During development, actin-monomer binding proteins, including profilin, and actin depolymerizing factor/cofilin regulate actin filament dynamics (Obinata, 1993;Obinata et al., 1997; Ono, 2003a,b). However, in mature myofibrils, these proteins are no longer major components of the thin filaments, and filament binding proteins, such as tropomyosin and ␣-actinin, and end-capping proteins, such as CapZ and tropomodulin, become the major actin-associated proteins. However, the list of actin binding proteins in muscle is still growing and cellular functions of many of these proteins are not clearly understood.Kettin is a large protein of 500-700 kDa found in the Z-discs and the I-bands of arthropod muscles (Bullard et al., 2000;Bullard et al., 2002Bullard et al., , 2006. Kettin directly binds to actin filaments with high-affinity (Lakey et al., 1993;Maki et al., 1995;van Straaten et al., 1999). Proteolytic removal of kettin by calpain from the Z-discs causes ...

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Based on sequence homology, a gene coding for a kettinlike protein has been found in the nematode Caenorhabditis elegans (Hakeda et al, 2000;Kolmerer et al, 2000). Transcripts of this gene are expressed in various muscle cells, and a monoclonal antibody (mAb) against insect kettin reacts with the dense bodies in obliquely striated body wall muscle (Kolmerer et al, 2000), which is equivalent to the Z-lines in cross-striated muscle.…”

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Caenorhabditis elegansKettin, a Large Immunoglobulin-like Repeat Protein, Binds to Filamentous Actin and Provides Mechanical Stability to the Contractile Apparatuses in Body Wall Muscle

Ono

Mohri

et al. 2006

MBoC

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Genetics of the Drosophila flight muscle myofibril: a window into the biology of complex systems

Vigoreaux

2001

BioEssays

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This essay reviews the long tradition of experimental genetics of the Drosophila indirect flight muscles (IFM). It discusses how genetics can operate in tandem with multidisciplinary approaches to provide a description, in molecular terms, of the functional properties of the muscle myofibril. In particular, studies at the interface of genetics and proteomics address protein function at the cellular scale and offer an outstanding platform with which to elucidate how the myofibril works. Two generalizations can be enunciated from the studies reviewed. First, the study of mutant IFM proteomes provides insight into how proteins are functionally organized in the myofibril. Second, IFM mutants can give rise to structural and contractile defects that are unrelated, a reflection of the dual function that myofibrillar proteins play as fundamental components of the sarcomeric framework and biochemical "parts" of the contractile "engine".

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The Contributions of Genetics to the Study of Insect Flight Muscle Function

Cripps

Nature’s Versatile Engine: Insect Flight Muscle Inside and Out

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Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans 1 1Edited by J. Karn

Cited by 43 publications

References 34 publications

Caenorhabditis elegansKettin, a Large Immunoglobulin-like Repeat Protein, Binds to Filamentous Actin and Provides Mechanical Stability to the Contractile Apparatuses in Body Wall Muscle

Caenorhabditis elegansKettin, a Large Immunoglobulin-like Repeat Protein, Binds to Filamentous Actin and Provides Mechanical Stability to the Contractile Apparatuses in Body Wall Muscle

Genetics of the Drosophila flight muscle myofibril: a window into the biology of complex systems

The Contributions of Genetics to the Study of Insect Flight Muscle Function

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