Structure and distribution of mini-titins

Vibert, Peter; York, Mary Lee; Castellani, Loriana; Edelstein, Stacey; Elliott, Bruce W.; Nyitray, László

doi:10.1016/0065-227x(96)81675-3

Cited by 12 publications

(5 citation statements)

References 33 publications

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“…In the only in vivo study, Siegman et al (1997Siegman et al ( , 1998 have found that the major phosphorylated protein during relaxation of Mytilus ABRM was a twitchin-related protein. However, all these proteins are common to both catch and non-catch muscles (Vibert et al, 1993(Vibert et al, , 1996. In this report, we have identi®ed a novel protein in molluscan muscles.…”

Section: Discussionmentioning

confidence: 78%

Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene

Yamada

Matsumoto

Oiwa

et al. 2000

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 78%

Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene

Yamada

Matsumoto

Oiwa

et al. 2000

Journal of Molecular Biology

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“…D-Titin represents the third Drosophila member of the titin gene family. The other two family members, both of which are referred to as mini-titins ( Vibert et al, 1996 ), include KETTIN and PROJECTIN. KETTIN is a 500-kD family member with low homology to vertebrate titin.…”

Section: Discussionmentioning

confidence: 99%

Human Autoantibodies Reveal Titin as a Chromosomal Protein

Machado

Sunkel

Andrew

1998

The Journal of Cell Biology

120

122

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Assembly of the higher-order structure of mitotic chromosomes is a prerequisite for proper chromosome condensation, segregation and integrity. Understanding the details of this process has been limited because very few proteins involved in the assembly of chromosome structure have been discovered. Using a human autoimmune scleroderma serum that identifies a chromosomal protein in human cells and Drosophila embryos, we cloned the corresponding Drosophila gene that encodes the homologue of vertebrate titin based on protein size, sequence similarity, developmental expression and subcellular localization. Titin is a giant sarcomeric protein responsible for the elasticity of striated muscle that may also function as a molecular scaffold for myofibrillar assembly. Molecular analysis and immunostaining with antibodies to multiple titin epitopes indicates that the chromosomal and muscle forms of titin may vary in their NH2 termini. The identification of titin as a chromosomal component provides a molecular basis for chromosome structure and elasticity.

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“…In bivalves, twitchin, which is also called mini-titin, has been found not only in smooth but also in striated muscles. 23,24 Here, by using our in vitro catch assay, we investigated oyster and scallop striated muscle twitchins and myosins, and found that they also had catchability.…”

Section: Introductionmentioning

confidence: 97%