| First Author | Pendlebury DF | Year | 2017 |
| Journal | Nat Struct Mol Biol | Volume | 24 |
| Issue | 12 | Pages | 1064-1072 |
| PubMed ID | 29083414 | Mgi Jnum | J:256440 |
| Mgi Id | MGI:6114239 | Doi | 10.1038/nsmb.3493 |
| Citation | Pendlebury DF, et al. (2017) Dissecting the telomere-inner nuclear membrane interface formed in meiosis. Nat Struct Mol Biol 24(12):1064-1072 |
| abstractText | Tethering telomeres to the inner nuclear membrane (INM) allows homologous chromosome pairing during meiosis. The meiosis-specific protein TERB1 binds the telomeric protein TRF1 to establish telomere-INM connectivity and is essential for mouse fertility. Here we solve the structure of the human TRF1-TERB1 interface to reveal the structural basis for telomere-INM linkage. Disruption of this interface abrogates binding and compromises telomere-INM attachment in mice. An embedded CDK-phosphorylation site within the TRF1-binding region of TERB1 provides a mechanism for cap exchange, a late-pachytene phenomenon involving the dissociation of the TRF1-TERB1 complex. Indeed, further strengthening this interaction interferes with cap exchange. Finally, our biochemical analysis implicates distinct complexes for telomere-INM tethering and chromosome-end protection during meiosis. Our studies unravel the structure, stoichiometry, and physiological implications underlying telomere-INM tethering, thereby providing unprecedented insights into the unique function of telomeres in meiosis. |
