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ITSN2L Interacts with and Negatively Regulates RABEP1

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 doma...

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Detalles Bibliográficos
Autores principales: Yang, Xiaoxu, Yan, Feng, He, Zhicheng, Liu, Shan, Cheng, Yeqing, Wei, Ke, Gan, Shiquan, Yuan, Jing, Wang, Shang, Xiao, Ye, Ren, Kaiqun, Liu, Ning, Hu, Xiang, Ding, Xiaofeng, Hu, Xingwang, Xiang, Shuanglin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4691038/
https://www.ncbi.nlm.nih.gov/pubmed/26633357
http://dx.doi.org/10.3390/ijms161226091
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author Yang, Xiaoxu
Yan, Feng
He, Zhicheng
Liu, Shan
Cheng, Yeqing
Wei, Ke
Gan, Shiquan
Yuan, Jing
Wang, Shang
Xiao, Ye
Ren, Kaiqun
Liu, Ning
Hu, Xiang
Ding, Xiaofeng
Hu, Xingwang
Xiang, Shuanglin
author_facet Yang, Xiaoxu
Yan, Feng
He, Zhicheng
Liu, Shan
Cheng, Yeqing
Wei, Ke
Gan, Shiquan
Yuan, Jing
Wang, Shang
Xiao, Ye
Ren, Kaiqun
Liu, Ning
Hu, Xiang
Ding, Xiaofeng
Hu, Xingwang
Xiang, Shuanglin
author_sort Yang, Xiaoxu
collection PubMed
description 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.
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spelling pubmed-46910382016-01-06 ITSN2L Interacts with and Negatively Regulates RABEP1 Yang, Xiaoxu Yan, Feng He, Zhicheng Liu, Shan Cheng, Yeqing Wei, Ke Gan, Shiquan Yuan, Jing Wang, Shang Xiao, Ye Ren, Kaiqun Liu, Ning Hu, Xiang Ding, Xiaofeng Hu, Xingwang Xiang, Shuanglin Int J Mol Sci Article 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. MDPI 2015-11-27 /pmc/articles/PMC4691038/ /pubmed/26633357 http://dx.doi.org/10.3390/ijms161226091 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Yang, Xiaoxu
Yan, Feng
He, Zhicheng
Liu, Shan
Cheng, Yeqing
Wei, Ke
Gan, Shiquan
Yuan, Jing
Wang, Shang
Xiao, Ye
Ren, Kaiqun
Liu, Ning
Hu, Xiang
Ding, Xiaofeng
Hu, Xingwang
Xiang, Shuanglin
ITSN2L Interacts with and Negatively Regulates RABEP1
title ITSN2L Interacts with and Negatively Regulates RABEP1
title_full ITSN2L Interacts with and Negatively Regulates RABEP1
title_fullStr ITSN2L Interacts with and Negatively Regulates RABEP1
title_full_unstemmed ITSN2L Interacts with and Negatively Regulates RABEP1
title_short ITSN2L Interacts with and Negatively Regulates RABEP1
title_sort itsn2l interacts with and negatively regulates rabep1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4691038/
https://www.ncbi.nlm.nih.gov/pubmed/26633357
http://dx.doi.org/10.3390/ijms161226091
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