Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation

Yuefeng Sun; Jianwei Sun; Panida Lungchukiet; Waise Quarni; Shengyu Yang; Xiaohong Zhang; Wenlong Bai

doi:10.1038/srep11529

Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation

Yuefeng Sun, Jianwei Sun, Panida Lungchukiet, Waise Quarni, Shengyu Yang, Xiaohong Zhang, Wenlong Bai

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Abstract

Fe65 is a brain-enriched adaptor protein known for its role in the action of the Aβ amyloid precursor protein in neuronal cells and Alzheimer's disease, but little is known about its functions in cancer cells. The present study documents for the first time a role of Fe65 in suppressing breast cancer cell migration and invasion. Mechanistic studies suggest that the suppression is mediated through its phosphotyrosine binding domain 1 that mediates the recruitment of Tip60 to cortactin to stimulate its acetylation. The studies identify the Tip60 acetyltransferase as a cytoplasmic drug target for the therapeutic intervention of metastatic breast cancers.

Original language	English (US)
Article number	11529
Journal	Scientific reports
Volume	5
DOIs	https://doi.org/10.1038/srep11529
State	Published - Jul 13 2015

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title = "Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation",

abstract = "Fe65 is a brain-enriched adaptor protein known for its role in the action of the Aβ amyloid precursor protein in neuronal cells and Alzheimer's disease, but little is known about its functions in cancer cells. The present study documents for the first time a role of Fe65 in suppressing breast cancer cell migration and invasion. Mechanistic studies suggest that the suppression is mediated through its phosphotyrosine binding domain 1 that mediates the recruitment of Tip60 to cortactin to stimulate its acetylation. The studies identify the Tip60 acetyltransferase as a cytoplasmic drug target for the therapeutic intervention of metastatic breast cancers.",

author = "Yuefeng Sun and Jianwei Sun and Panida Lungchukiet and Waise Quarni and Shengyu Yang and Xiaohong Zhang and Wenlong Bai",

note = "Funding Information: The studies were supported by an Idea Award from the Breast Cancer Research Program of US Department of Defense W81XWH-09-1-0574 (to W. Bai) and a NIH Public Health Service grants CA111334 (to W. Bai) and CA164147 (to X. Zhang).",

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doi = "10.1038/srep11529",

language = "English (US)",

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T1 - Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation

AU - Sun, Yuefeng

AU - Sun, Jianwei

AU - Lungchukiet, Panida

AU - Quarni, Waise

AU - Yang, Shengyu

AU - Zhang, Xiaohong

AU - Bai, Wenlong

N1 - Funding Information: The studies were supported by an Idea Award from the Breast Cancer Research Program of US Department of Defense W81XWH-09-1-0574 (to W. Bai) and a NIH Public Health Service grants CA111334 (to W. Bai) and CA164147 (to X. Zhang).

PY - 2015/7/13

Y1 - 2015/7/13

N2 - Fe65 is a brain-enriched adaptor protein known for its role in the action of the Aβ amyloid precursor protein in neuronal cells and Alzheimer's disease, but little is known about its functions in cancer cells. The present study documents for the first time a role of Fe65 in suppressing breast cancer cell migration and invasion. Mechanistic studies suggest that the suppression is mediated through its phosphotyrosine binding domain 1 that mediates the recruitment of Tip60 to cortactin to stimulate its acetylation. The studies identify the Tip60 acetyltransferase as a cytoplasmic drug target for the therapeutic intervention of metastatic breast cancers.

AB - Fe65 is a brain-enriched adaptor protein known for its role in the action of the Aβ amyloid precursor protein in neuronal cells and Alzheimer's disease, but little is known about its functions in cancer cells. The present study documents for the first time a role of Fe65 in suppressing breast cancer cell migration and invasion. Mechanistic studies suggest that the suppression is mediated through its phosphotyrosine binding domain 1 that mediates the recruitment of Tip60 to cortactin to stimulate its acetylation. The studies identify the Tip60 acetyltransferase as a cytoplasmic drug target for the therapeutic intervention of metastatic breast cancers.

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Fe65 Suppresses Breast Cancer Cell Migration and Invasion through Tip60 Mediated Cortactin Acetylation

Abstract

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