To the Editor : We read with great interest the article by Sasa et al. (1) in which they identified three novel truncating mutations in the telomere‐associated protein TIN2 in children with an inherited form of bone‐marrow failure syndrome known as Dyskeratosis congenita (DC). TIN2 is one of the six protein subunits of the shelterin protein complex that binds to telomeric sequences at chromosome ends to maintain genome structural integrity and to regulate telomere lengths (2, 3) . In this complex, TIN2 protein directly interacts with TRF1, TRF2 and TPP1 ( Fig. 1a ). 1 ( a ) A model of the shelterin protein complex on telomeric DNA. Co‐immunoprecipitation analyses of TIN2 protein variants with ( b ) TRF1, ( c ) TRF2, and ( d ) TPP1. The co‐immunoprecipitated samples are denoted as IP, whereas cell lysates used prior to co‐immunoprecipitation (i.e. input samples) are denoted as WB. Due to the fact that some TIN2 mutants shown in panel ( c ) (i.e. L287P, R289S and R291G) appeared to show some defects in association with TRF2, a repeated co‐immunoprecipitation reaction was performed between TRF2 and those TIN2 mutants only ( e ). The results ( f )
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Characterization of interactions between naturally mutated forms of the TIN2 protein and its known protein partners of the shelterin complex
Xin, Z‐T; Ly, H
Follow Clinical Genetics
, Volume 81 (3)
Wiley – Mar 1, 2012
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