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最后，还是 POT1：磷酸化使人类端粒蛋白 POT1 能够招募富含 C 的链端复制机制。

At the end, it is POT1 again: Phosphorylation allows human telomeric protein POT1 to recruit the C-rich strand end replication machinery.

机构信息

Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

出版信息

Mol Cell. 2024 Jul 25;84(14):2598-2600. doi: 10.1016/j.molcel.2024.06.030.

DOI:10.1016/j.molcel.2024.06.030
PMID:39059369
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11613731/
Abstract

Recently in Cell, Cai et al. reported how phosphorylation of human shelterin protein POT1 allows it to recruit the telomeric C-rich strand replication machinery, providing mechanistic insights into an understudied area of telomere biology with implications for telomere biology disorders.

摘要

最近，在《细胞》杂志上，蔡等人报告了人类庇护蛋白 POT1 的磷酸化如何使其能够招募端粒的 C 丰富链复制机制，为端粒生物学中一个研究不足的领域提供了机制上的见解，这对端粒生物学紊乱具有重要意义。

相似文献

[1]
At the end, it is POT1 again: Phosphorylation allows human telomeric protein POT1 to recruit the C-rich strand end replication machinery.

Mol Cell. 2024-7-25

[2]
POT1 recruits and regulates CST-Polα/primase at human telomeres.

Cell. 2024-7-11

[3]
Comparison of Telomere Structure in Eukaryotes.

Arch Razi Inst. 2024-12-31

[4]
TRF2 promotes dynamic and stepwise looping of POT1 bound telomeric overhang.

Nucleic Acids Res. 2021-12-2

[5]
The human telomeric proteome during telomere replication.

Nucleic Acids Res. 2021-12-2

[6]
Human shelterin protein POT1 prevents severe telomere instability induced by homology-directed DNA repair.

EMBO J. 2020-12-1

[7]
Shelterin proteins and cancer.

Asian Pac J Cancer Prev. 2015

[8]
TERRA and hnRNPA1 orchestrate an RPA-to-POT1 switch on telomeric single-stranded DNA.

Nature. 2011-3-13

[9]
Structural and functional analysis of the human POT1-TPP1 telomeric complex.

Nat Commun. 2017-4-10

[10]
Shelterin reduces the accessibility of telomeric overhangs.

Nucleic Acids Res. 2022-12-9

本文引用的文献

[1]
POT1 recruits and regulates CST-Polα/primase at human telomeres.

Cell. 2024-7-11

[2]
Human POT1 protects the telomeric ds-ss DNA junction by capping the 5' end of the chromosome.

Science. 2023-8-18

[3]
Structures of the human CST-Polα-primase complex bound to telomere templates.

Nature. 2022-8

[4]
Cryo-EM structure of the human CST-Polα/primase complex in a recruitment state.

Nat Struct Mol Biol. 2022-8

[5]
Distinct functions of POT1 proteins contribute to the regulation of telomerase recruitment to telomeres.

Nat Commun. 2021-9-17

[6]
The structure of human CST reveals a decameric assembly bound to telomeric DNA.

Science. 2020-6-5

[7]
Telomeric 3' overhangs derive from resection by Exo1 and Apollo and fill-in by POT1b-associated CST.

Cell. 2012-6-28

[8]
OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation.

J Biol Chem. 2009-9-25

[9]
TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase.

Nature. 2007-2-1

[10]
Pot1, the putative telomere end-binding protein in fission yeast and humans.

Science. 2001-5-11

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