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Dual roles of TRF1 in tethering telomeres to the nuclear envelope and protecting them from fusion during meiosis

Artikel i vetenskaplig tidskrift
Författare L. N. Wang
Zhaowei Tu
C. Liu
H. B. Liu
P. Kaldis
Z. J. Chen
W. Li
Publicerad i Cell Death and Differentiation
Volym 25
Nummer/häfte 6
Sidor 1174-1188
ISSN 1350-9047
Publiceringsår 2018
Publicerad vid Institutionen för kemi och molekylärbiologi
Sidor 1174-1188
Språk en
Länkar doi.org/10.1038/541418-017-0037-8
Ämnesord meiotic prophase, genome instability, end-protection, germ-cells, dna, protein, complex, chromosomes, mice, shelterin, Biochemistry & Molecular Biology, Cell Biology
Ämneskategorier Cellbiologi, Biokemi och molekylärbiologi

Sammanfattning

Telomeres integrity is indispensable for chromosomal stability by preventing chromosome erosion and end-to-end fusions. During meiosis, telomeres attach to the inner nuclear envelope and cluster into a highly crowded microenvironment at the bouquet stage, which requires specific mechanisms to protect the telomeres from fusion. Here, we demonstrate that germ cell-specific knockout of a shelterin complex subunit, Ttf1, results in arrest of spermatocytes at two different stages. The obliterated telomere-nuclear envelope attachment in Trf1/-deficient spermatocytes impairs homologue synapsis and recombination, resulting in a pachytene-like arrest, while the meiotic division arrest might stem from chromosome end-to end fusion due to the failure of recruiting meiosis specific telomere associated proteins. Further investigations uncovered that TRF1 could directly interact with Speedy A, and Speedy A might work as a scaffold protein to further recruit Cdk2, thus protecting telomeres from fusion at this stage. Together, our results reveal a novel mechanism of TRF1, Speedy A, and Cdk2 in protecting telomere from fusion in a highly crowded microenvironment during meiosis.

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