Scholarlink

<p>The Telomere Repeat-Binding factor 2 (TRF2) contributes to cancer progression by both telomere-dependent and independent mechanisms, including immune escape and angiogenesis. Here, we found that TRF2, through its Basic domain, directly interacts with Emerin forming a complex, including Lamin A/C, Lamin B1, SUN1, and SUN2. Importantly, TRF2 association with the inner nuclear membrane is functional to the proper establishment of cell polarity, finally promoting productive 1D and 3D migration in triple negative breast cancer cells (TNBC). In line with this, a spontaneous model of TNBC metastasis, combined with intravital imaging, allowed us to demonstrate that TRF2 promotes cell migration at the primary tumor site and is required for the early steps of the metastatic cascade. In human breast cancers, aberrantly elevated TRF2 expression positively correlates with cancer progression, metastasis, and poor prognosis, identifying TRF2 as a potential target for novel therapeutic strategies against TNBC.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

TRF2 interaction with nuclear envelope is required for cell polarization and metastasis in triple negative breast cancer

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年3月30日

查看全文
  • Eleonora Petti,
  • Serena Di Vito,
  • Roberto Dinami,
  • Manuela Porru,
  • Stefano Marchesi,
  • Jeroen Lohuis,
  • Pasquale Zizza,
  • Sara Iachettini,
  • Erica Salvati,
  • Carmen D’Angelo,
  • Angela Rizzo,
  • Carmen Maresca,
  • Flora Ascione,
  • Anna Di Benedetto,
  • Simonetta Buglioni,
  • Andrea Sacconi,
  • Paola Ostano,
  • Qingsen Li,
  • Antonella Stoppacciaro,
  • Carlo Leonetti,
  • Jacco van Rheenen,
  • Paolo Maiuri,
  • Giorgio Scita,
  • Annamaria Biroccio

摘要

The Telomere Repeat-Binding factor 2 (TRF2) contributes to cancer progression by both telomere-dependent and independent mechanisms, including immune escape and angiogenesis. Here, we found that TRF2, through its Basic domain, directly interacts with Emerin forming a complex, including Lamin A/C, Lamin B1, SUN1, and SUN2. Importantly, TRF2 association with the inner nuclear membrane is functional to the proper establishment of cell polarity, finally promoting productive 1D and 3D migration in triple negative breast cancer cells (TNBC). In line with this, a spontaneous model of TNBC metastasis, combined with intravital imaging, allowed us to demonstrate that TRF2 promotes cell migration at the primary tumor site and is required for the early steps of the metastatic cascade. In human breast cancers, aberrantly elevated TRF2 expression positively correlates with cancer progression, metastasis, and poor prognosis, identifying TRF2 as a potential target for novel therapeutic strategies against TNBC.