Group:MUZIC:Telethonin

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Studies on telethonin structure by Zou et al. <ref>PMID:16407954</ref> report that it is made up of <scene name='User:Marcia_Ivonne_Pena_Paz/workbench/Telethonin/Telethonin_nter_cter/1'>five stranded antiparallel β-sheets extended by two wing-shaped β-hairpin motifs (A-B, C-D). These two motifs are related by an approximate two-fold symmetry, which generates an almost perfect palindromic arrangement.</scene> (N-terminal in blue and C-ter in orange)
Studies on telethonin structure by Zou et al. <ref>PMID:16407954</ref> report that it is made up of <scene name='User:Marcia_Ivonne_Pena_Paz/workbench/Telethonin/Telethonin_nter_cter/1'>five stranded antiparallel β-sheets extended by two wing-shaped β-hairpin motifs (A-B, C-D). These two motifs are related by an approximate two-fold symmetry, which generates an almost perfect palindromic arrangement.</scene> (N-terminal in blue and C-ter in orange)
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The structure of telethonin was determined using X-ray crystallography <ref>PMID:12446666</ref>,<ref>PMID:16407954</ref> . The shape and architecture of the complex of titin/telethonin was studied by small-angle- X-ray scattering (SAXS) and then compared to the crystallographic models. They also used in-vitro experiments to follow the formation of the complex in non-myogenic Cos1 cells, in order to understand if the assemblage is possible <ref>PMID:16713295</ref>
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The structure of telethonin was determined using X-ray crystallography. <ref>PMID:12446666</ref>,<ref name="a"> PMID:16678796 </ref> The shape and architecture of the complex of titin/telethonin was studied by small-angle- X-ray scattering (SAXS) and then compared to the crystallographic models. They also used in-vitro experiments to follow the formation of the complex in non-myogenic Cos1 cells, in order to understand if the assemblage is possible <ref>PMID:16713295</ref>
This symmetry of telethonin permits its interaction with titin. Both are assembled in an antiparallel <scene name='User:Marcia_Ivonne_Pena_Paz/workbench/Telethonin/Telethonin-titin/1'>sandwich 2:1</scene> (titin:telethonin). Titin N-terminal domains Z1 and Z2 (two Ig like repeats) interact with the C-terminal region of telethonin (residues 1-53). Telethonin mediates in the antiparallel assembly of the two Z1Z2domains.
This symmetry of telethonin permits its interaction with titin. Both are assembled in an antiparallel <scene name='User:Marcia_Ivonne_Pena_Paz/workbench/Telethonin/Telethonin-titin/1'>sandwich 2:1</scene> (titin:telethonin). Titin N-terminal domains Z1 and Z2 (two Ig like repeats) interact with the C-terminal region of telethonin (residues 1-53). Telethonin mediates in the antiparallel assembly of the two Z1Z2domains.
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Telethonin is also involved in signalling processes that regulate muscle development. A feed back loop is formed with MRFs (MyoD, myogenin, Myf5) regulating Tcap gene expression; telethonin interacts with myostatin, inhibiting it. So it regulates MyoD through the Myostatin – Smad3 pathway. <ref>PMID:18440815</ref>.
Telethonin is also involved in signalling processes that regulate muscle development. A feed back loop is formed with MRFs (MyoD, myogenin, Myf5) regulating Tcap gene expression; telethonin interacts with myostatin, inhibiting it. So it regulates MyoD through the Myostatin – Smad3 pathway. <ref>PMID:18440815</ref>.
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There is an interaction with MDM2 N-terminal. MDM2 is capable of redirecting telethonin to the nucleus. Telethonin is inhibited by MDM2 in a dose dependent manner. In cells MDM2 is involved in the regulation of proteasomal turnover of telethonin. <ref>PMID:16678796 </ref>
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There is an interaction with MDM2 N-terminal. MDM2 is capable of redirecting telethonin to the nucleus. Telethonin is inhibited by MDM2 in a dose dependent manner. In cells MDM2 is involved in the regulation of proteasomal turnover of telethonin. <ref name="a" />
Another interaction has been reported, and also associated with pathology, the one with bone morphogenetic protein-10 (BMP10). The interaction of telethonin with BMP10 is described as a sensor of increased wall stress of the left ventricle. A BMP10 variant is associated with hypertension dilated cardiomyopathy; its binding to telethonin is reduced, and its extracellular secretion is increased, causing cardiomyocyte hypertrophy. <ref>PMID:17921333 </ref>
Another interaction has been reported, and also associated with pathology, the one with bone morphogenetic protein-10 (BMP10). The interaction of telethonin with BMP10 is described as a sensor of increased wall stress of the left ventricle. A BMP10 variant is associated with hypertension dilated cardiomyopathy; its binding to telethonin is reduced, and its extracellular secretion is increased, causing cardiomyocyte hypertrophy. <ref>PMID:17921333 </ref>

Revision as of 11:44, 22 August 2011

Telethonin

Telethonin crystal structure by Zou et al. (2006) interacting with Z1 and Z2 titin domains(PDB entry 1ya5)

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Proteopedia Page Contributors and Editors (what is this?)

Marcia Ivonne Peña Paz, Nikos Pinotsis, Jaime Prilusky

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