| First Author | Zhang J | Year | 2017 |
| Journal | Cell Rep | Volume | 21 |
| Issue | 7 | Pages | 1715-1726 |
| PubMed ID | 29141207 | Mgi Jnum | J:315957 |
| Mgi Id | MGI:6831847 | Doi | 10.1016/j.celrep.2017.10.061 |
| Citation | Zhang J, et al. (2017) Distinct TERB1 Domains Regulate Different Protein Interactions in Meiotic Telomere Movement. Cell Rep 21(7):1715-1726 |
| abstractText | Meiotic telomeres attach to the nuclear envelope (NE) and drive the chromosome movement required for the pairing of homologous chromosomes. The meiosis-specific telomere proteins TERB1, TERB2, and MAJIN are required to regulate these events, but their assembly processes are largely unknown. Here, we developed a germ-cell-specific knockout mouse of the canonical telomere-binding protein TRF1 and revealed an essential role for TRF1 in directing the assembly of TERB1-TERB2-MAJIN. Further, we identified a TERB2 binding (T2B) domain in TERB1 that is dispensable for the TRF1-TERB1 interaction but is essential for the subsequent TERB1-TERB2 interaction and therefore for telomere attachment to the NE. Meanwhile, cohesin recruitment at telomeres, which is required for efficient telomere movement, is mediated by the MYB-like domain of TERB1, but not by TERB2-MAJIN. Our results reveal distinct protein interactions through various domains of TERB1, which enable the sequential assembly of the meiotic telomere complex for their movements. |
