scholarly journals Upregulated SLC27A2/FATP2 in differentiated thyroid carcinoma promotes tumor proliferation and migration

Author(s):  
Kaixiang Feng ◽  
Runsheng Ma ◽  
Hongqiang Li ◽  
Keyu Yin ◽  
Gongbo Du ◽  
...  
2021 ◽  
Author(s):  
Wei‐Jun Zhao ◽  
Liu‐Lian Zhu ◽  
Wei‐Qiang Yang ◽  
Shuai‐Jun Xu ◽  
Jie Chen ◽  
...  

2021 ◽  
Author(s):  
Jun Tian ◽  
Bei Li ◽  
Jing Qiao ◽  
Xinfeng Pang ◽  
Xiaojing Yue

Abstract Background: Programmed cell death protein 4 (PDCD4), which serves as a tumor suppressor protein, plays a important role in cell proliferation,apoptosis, cell migration and DNA-damage response.However, the exact mechanism for the deubiquitination of PDCD4 remain unclear.Methods: Western blotting was used to detect the expression of PDCD4 in the breast cancer tissues and BC cell lines. We identified the potential PDCD4 associated deubiquitinase by RNAi screening. GST-Pull down and domain-mapping analysis were used to reveal that USP13 and PDCD4 directly interact with each other.Flow cytometry was used to detect the changes of G1 to S phase. Soft agar assay was used to measure the changes of the cell proliferation efficiency.Results: The expression of PDCD4 was decreased in the breast cancer tissues and BC cell lines. USP13 as a potential PDCD4 associated deubiquitinase. USP13 physically interacted with PDCD4 and greatly increased the steady state of PDCD4 through the ubiquitin-proteasome pathway.Importantly, silencing of the USP13 facilitated cell cycle from G1 to Sphase, promoted breast tumor cells proliferation and migration through downregulation of PDCD4. Conclusions: Together, these results suggest that USP13 plays an important role in the breast tumor proliferation and migration through modulating PDCD4 stability.


2015 ◽  
Vol 33 (3) ◽  
pp. 1402-1410 ◽  
Author(s):  
XIAO-WEI WANG ◽  
XUE-QIN XI ◽  
JIAN WU ◽  
YI-YUAN WAN ◽  
HONG-XIA HUI ◽  
...  

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