Year: 2010
Type: article
Abstract: 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 NFκB 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.
Source: Cell Cycle
Authors: Shaheen Kabir, Agnel Sfeir, Titia de Lange
Institution: Rockefeller University
Language: English
Subfield: Physiology (medical)
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Awards: Mechanism of the telomeric proliferation limit, Molecular Cytology of Human Telomeres: Telomere protein, G2687155412, Telomere length control by shelterin, Molecular cytology of human telomeres-telomere protein, G7307501964, G895249668, G9000140848, Mechanism of the telomeric proliferation limit
OpenAlex ID: W2152598515