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Dev Dyn 2010 Apr 01;2394:1124-35. doi: 10.1002/dvdy.22263.
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Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance.

Sadikot T , Hammond CR , Ferrari MB .

The N-terminus of telethonin forms a unique structure linking two titin N-termini at the Z-disc. While a specific role for the C-terminus has not been established, several studies indicate it may have a regulatory function. Using a morpholino approach in Xenopus, we show that telethonin knockdown leads to embryonic paralysis, myocyte defects, and sarcomeric disruption. These myopathic defects can be rescued by expressing full-length telethonin mRNA in morpholino background, indicating that telethonin is required for myofibrillogenesis. However, a construct missing C-terminal residues is incapable of rescuing motility or sarcomere assembly in cultured myocytes. We, therefore, tested two additional constructs: one where four C-terminal phosphorylatable residues were mutated to alanines and another where terminal residues were randomly replaced. Data from these experiments support that the telethonin C-terminus is required for assembly, but in a context-dependent manner, indicating that factors and forces present in vivo can compensate for C-terminal truncation or mutation.

PubMed ID: 20235223
Article link: Dev Dyn

Species referenced: Xenopus
Genes referenced: acta1 actl6a actn1 actn2 myc tcap ttn
Antibodies: Actn2 Ab1 Fluro-phalloidin Ab Myc Ab3 Myh1 Ab1 Ttn Ab1
Morpholinos: tcap MO1

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