Taking apart Rap1 An adaptor protein with telomeric and non-telomeric functions

被引:28
作者
Kabir, Shaheen [1 ]
Sfeir, Agnel [1 ]
de lange, Titia [1 ]
机构
[1] Rockefeller Univ, Cell Biol & Genet Lab, New York, NY 10021 USA
关键词
telomere; Rap1; shelterin; transcription; NF kappa B signaling; homology-directed repair; non-homologous end-joining; BINDING-PROTEIN; DNA; YEAST; END; TRF2; COMPLEX; RECOMBINATION; GENE; MAINTENANCE; PROTECTION;
D O I
10.4161/cc.9.20.13579
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Mammalian Rap1, a TRF2-interacting protein in the telomeric shelterin complex, was recently shown to repress homology-directed repair at chromosome ends. In addition, Rap1 plays a role in transcriptional regulation and NF kappa B signaling. Rap1 is unique among the components of shelterin in that it is conserved in budding yeast and has non-telomeric functions. Comparison of mammalian Rap1 to the Rap1 proteins of several budding yeasts and fission yeast reveal both striking similarities and notable differences. The protean nature of Rap1 is best understood by viewing it as an adaptor that can mediate a variety of protein-protein and protein-DNA interactions depending on the organism and the complex in which it is functioning.
引用
收藏
页码:4061 / 4067
页数:7
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