Sandbox Reserved 1103: Difference between revisions

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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>.

Finally, TIN2 seems to regulate the effect of the tankyrase 1, an poly ADP-ribose polymerase, by stabilising the formation of a TIN2–tankyrase 1–TRF1 complex. This prevent the binding of TRF1 to the telomere ends. In the case of amino acid mutations in TIN2 this might act by the same mechanism as a knock-down and leave telomere ends permanently unprotected, causing a shortening of telomere length <ref>PMID: 19419704 </ref>.

Finally, TIN2 seems to regulate the effect of the [https://en.wikipedia.org/wiki/Tankyrase tankyrase 1], an poly ADP-ribose polymerase, by stabilising the formation of a TIN2–tankyrase 1–TRF1 complex. This prevent the binding of TRF1 to the telomere ends. In the case of amino acid mutations in TIN2 this might act by the same mechanism as a knock-down and leave telomere ends permanently unprotected, causing a shortening of telomere length <ref>PMID: 19419704 </ref>.

=== Revesz syndrome ===

Sandbox Reserved 1103: Difference between revisions

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@@ Line 38: / Line 38: @@
 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>.
-Finally, TIN2 seems to regulate the effect of the tankyrase 1, an poly ADP-ribose polymerase, by stabilising the formation of a TIN2–tankyrase 1–TRF1 complex. This prevent the binding of TRF1 to the telomere ends. In the case of amino acid mutations in TIN2 this might act by the same mechanism as a knock-down and leave telomere ends permanently unprotected, causing a shortening of telomere length <ref>PMID: 19419704 </ref>.
+Finally, TIN2 seems to regulate the effect of the [https://en.wikipedia.org/wiki/Tankyrase tankyrase 1], an poly ADP-ribose polymerase, by stabilising the formation of a TIN2–tankyrase 1–TRF1 complex. This prevent the binding of TRF1 to the telomere ends. In the case of amino acid mutations in TIN2 this might act by the same mechanism as a knock-down and leave telomere ends permanently unprotected, causing a shortening of telomere length <ref>PMID: 19419704 </ref>.
 === Revesz syndrome ===