ITSN2L Interacts with and Negatively Regulates RABEP1

International Journal of Molecular Sciences

Xiaoxu Yang¹  Feng Yan¹  Zhicheng He¹  Shan Liu¹  Yeqing Cheng¹  Ke Wei¹  Shiquan Gan¹  Jing Yuan¹  Shang Wang¹  Ye Xiao¹  Kaiqun Ren¹  Ning Liu¹  Xiang Hu¹  Xiaofeng Ding¹  Xingwang Hu¹  Shuanglin Xiang¹ 

[1] Key Laboratory of Protein Chemistry and Developmental Biology of State Ministry of Education, College of Life Sciences, Hunan Normal University, Changsha 410081, China;

关键词: ITSN2L;    RABEP1;    endocytosis;    endosome;    interactions;   

DOI  :  10.3390/ijms161226091

来源: mdpi

【 摘 要 】

Intersectin-2Long (ITSN2L) is a multi-domain protein participating in endocytosis and exocytosis. In this study, RABEP1 was identified as a novel ITSN2L interacting protein using a yeast two-hybrid screen from a human brain cDNA library and this interaction, specifically involving the ITSN2L CC domain and RABEP1 CC3 regions, was further confirmed by in vitro GST (glutathione-S-transferase) pull-down and in vivo co-immunoprecipitation assays. Corroboratively, we observed that these two proteins co-localize in the cytoplasm of mammalian cells. Furthermore, over-expression of ITSN2L promotes RABEP1 degradation and represses RABEP1-enhanced endosome aggregation, indicating that ITSN2L acts as a negative regulator of RABEP1. Finally, we showed that ITSN2L and RABEP1 play opposite roles in regulating endocytosis. Taken together, our results indicate that ITSN2L interacts with RABEP1 and stimulates its degradation in regulation of endocytosis.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.