Sandbox GGC5: Difference between revisions
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== '''Function''' == | == '''Function''' == | ||
Titin, in its longest isoform, has a molecular weight exceeding 3 MDa and is over 1.5 μm in length. Titin typically contains immunoglobulin (Ig) domains which are typically 110 amino acids in length, contain an internal disulfide bond and two layers of β-pleated sheets.<ref>PMID:31856237</ref> On the cellular level, titin is typically located within the nucleus of the cell; however, it can also be located within the cytoplasm. | |||
Titin is a key component in the assembly and function of vertebrate striated muscles. Titin provides connections at the level of individual micro-filaments and contributes to the fine balance of forces between the two halves of the sarcomere. | Titin is a key component in the assembly and function of vertebrate striated muscles. Titin provides connections at the level of individual micro-filaments and contributes to the fine balance of forces between the two halves of the sarcomere. | ||
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In non-muscle cells, titin plays a role in chromosome condensation and chromosome segregation during mitosis. | In non-muscle cells, titin plays a role in chromosome condensation and chromosome segregation during mitosis. | ||
Protein kinase, including titin kinase, is a vital aspect of controlling cell proliferation and cell differentiation. Titin kinase is expressed in muscles and is responsible for the interaction with thick filaments known as myosin filaments. The enzymatic activity of protein kinases must be highly regulated through the phosphorylation of specific residues located in the activation component of the catalytic domain. Titin kinase is regulated in a two-step process including the partial unfolding of an inhibitory segment to expose the catalytic region followed by the phosphorylation of the Tyrosin residue. This tyrosine residue is depicted in the structural highlights listed below. <ref>PMID:19108772</ref>,<ref>PMID:9804419</ref> | Protein kinase, including titin kinase, is a vital aspect of controlling cell proliferation and cell differentiation. Titin kinase is expressed in muscles and is responsible for the interaction with thick filaments known as myosin filaments. The enzymatic activity of protein kinases must be highly regulated through the phosphorylation of specific residues located in the activation component of the catalytic domain. Titin kinase is regulated in a two-step process including the partial unfolding of an inhibitory segment to expose the catalytic region followed by the phosphorylation of the Tyrosin residue. This tyrosine residue is depicted in the structural highlights listed below. <ref>PMID:19108772</ref>,<ref>PMID:9804419</ref> | ||
