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Syntaxin 6-mediated Golgi translocation plays an important role in nuclear functions of EGFR through

Y Du1, J Shen1, J L Hsu2

  • 11] Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA [2] The University of Texas Graduate School of Biomedical Sciences at Houston, Houston, TX, USA.

Oncogene
|February 5, 2013
PubMed

Insights

This study reveals how epidermal growth factor receptor (EGFR) travels to the Golgi via microtubules and dynein, a key step for its nuclear functions in cancer. This uncovers a critical pathway for EGFR trafficking.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Receptor tyrosine kinases (RTKs) like EGFR are crucial cell surface receptors involved in signaling.
  • Abnormal RTK expression and trafficking are implicated in tumorigenesis.
  • While RTK intracellular trafficking is known, the cell surface-to-Golgi pathway remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of epidermal growth factor receptor (EGFR) intracellular trafficking from the cell surface to the Golgi apparatus.
  • To investigate the role of microtubules, dynein, and syntaxin 6 in EGFR Golgi translocation.
  • To determine the necessity of this trafficking pathway for EGFR's subsequent nuclear translocation and function.

Main Methods:

  • Investigated EGF-induced EGFR translocation using cell-based assays.
  • Utilized microscopy and biochemical methods to analyze microtubule-dependent movement and protein interactions.
  • Examined the role of dynein and syntaxin 6 in EGFR trafficking to the Golgi.
  • Assessed the impact of Golgi translocation on EGFR nuclear localization and function.

Main Results:

  • EGF stimulation triggers EGFR to move towards the Golgi apparatus.
  • EGFR translocation to the Golgi depends on microtubule-dependent transport involving dynein.
  • Syntaxin 6 mediates the fusion of EGFR-containing vesicles with the Golgi.
  • This Golgi translocation is essential for EGFR's subsequent movement to the nucleus and its nuclear functions.

Conclusions:

  • A novel mechanism for EGFR trafficking from the cell surface to the Golgi via microtubules and dynein has been identified.
  • Syntaxin 6 plays a critical role in mediating EGFR fusion with the Golgi.
  • The cell surface-to-Golgi-to-nucleus trafficking route is essential for EGFR's nuclear functions.
  • This pathway provides a comprehensive understanding of EGFR intracellular transport in physiological and pathological contexts.

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