Sandbox Reserved 1103: Difference between revisions
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Dyskeratosis congenita is a disorder which is characterised by bone marrow dysfunction, abnormality of the skin, mucocutaneous triad of oral leucoplakia, nail dystrophy, as well as a predisposition to cancer. | Dyskeratosis congenita is a disorder which is characterised by bone marrow dysfunction, abnormality of the skin, mucocutaneous triad of oral leucoplakia, nail dystrophy, as well as a predisposition to cancer. | ||
TINF2 is one of the nine identified genes that when mutated are related to the Dyskeratosis congenita, the others being DKC1, TERC, TERT, NOP10, NHP2 | TINF2 is one of the nine identified genes that when mutated are related to the Dyskeratosis congenita, the others being [https://en.wikipedia.org/wiki/Dyskerin DKC1],[https://en.wikipedia.org/wiki/Telomerase_RNA_component TERC],[https://en.wikipedia.org/wiki/Telomerase_reverse_transcriptase TERT], NOP10, NHP2, C16orf57, TCAB1 and [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN]. | ||
The majority of identified TIN2 dyskeratosis congenita mutations cluster is a highly conserved 30-amino-acid region near the ends of its TRF1 binding domain <ref>PMID: 15316005 </ref>, from position 270 to 300, located eight amino acids C-terminal to the FxLxP motif. A disrutpion of this domain causes a loss of TRF1 binding to TIN2, resulting in a telomeric instability<ref>PMID: 18252230 </ref>. Another proposal is that TIN2 help TPP1, another component of the shelterin complex, in the recruitment of telomerase through an unknown mechanism that is disrupted by the TIN2 dyskeratosis congenita mutations, leading once again to a telomeric instability <ref>PMID: 18252230 </ref>. | The majority of identified TIN2 dyskeratosis congenita mutations cluster is a highly conserved 30-amino-acid region near the ends of its TRF1 binding domain <ref>PMID: 15316005 </ref>, from position 270 to 300, located eight amino acids C-terminal to the FxLxP motif. A disrutpion of this domain causes a loss of TRF1 binding to TIN2, resulting in a telomeric instability<ref>PMID: 18252230 </ref>. Another proposal is that TIN2 help TPP1, another component of the shelterin complex, in the recruitment of telomerase through an unknown mechanism that is disrupted by the TIN2 dyskeratosis congenita mutations, leading once again to a telomeric instability <ref>PMID: 18252230 </ref>. | ||
