The shelterin component TPP1 is a binding partner and substrate for the deubiquitinating enzyme USP7.

ABSTRACT: The telomeric shelterin component TPP1 has critical functions in telomeric protein complex assembly and telomerase recruitment and regulation. Here we identify USP7 as a novel interacting protein of the oligonucleotide/oligosaccharide-binding fold of TPP1, which was previously known to recruit telomerase to telomeres. We identify amino acids in TPP1 and USP7 that are critical for their interaction and multiple lysines within TPP1 that are oligo-ubiquitinated and deubiquitinated by USP7. Mutational analysis indicated that human TPP1 does not require ubiquitination for telomere association in contrast to previous observations reported for mouse Tpp1. Ubiquitination of human TPP1 also had no detectable effects on known protein interactions of TPP1 with TIN2, POT1, the CTC1-STN1-TEN1 complex,

SUBMITTER: Zemp I 

PROVIDER: S-EPMC4192509 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature