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Defective Anks1a disrupts the export of receptor tyrosine kinases from the endoplasmic reticulumopen access

Authors
Park, Soochul
Issue Date
Dec-2016
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Keywords
Anks1a; Breast tumor; ErbB2 (HER2, neu); PTB adaptor
Citation
BMB REPORTS, v.49, no.12, pp 651 - 652
Pages
2
Journal Title
BMB REPORTS
Volume
49
Number
12
Start Page
651
End Page
652
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/9330
DOI
10.5483/BMBRep.2016.49.12.186
ISSN
1976-6696
1976-670X
Abstract
EphA2 has been implicated in amplifying ErbB2 tumorigenic signaling. One protein that interacts with EphA2 is the Anks1a PTB adaptor. However, the precise role of Anks1a in EphA2mediated tumorigenesis is unclear. We demonstrated that Anks1a localizes to the ER upon phosphorylation and that the Ankyrin repeats and PTB of Anks1a bind to EphA2 and Sec23, respectively. Thus, Anks1a facilitates the selective packaging of EphA2 into COPII vesicles. Additionally, Anks1a knockout mice, a phenocopy of EphA2 knockout mice, exhibited markedly reduced ErbB2-induced breast tumorigenesis. Strikingly, ErbB2 did not localize to the cell surface following Anks1a knock-down in primary mammary tumor cells over-expressing ErbB2. Importantly, EphA2 was critical for stabilizing ErbB2 through complex formation, but its interaction with Anks1a also facilitated ErbB2 loading into COPII carriers. These findings suggest a novel role for Anks1a in the molecular pathogenesis of breast tumors and possibly other human diseases.
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이과대학 (생명시스템학부)
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