상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

HAX1 regulates E3 ubiquitin ligase activity of cIAPs by promoting their dimerization

 

HAX1의 이합체화로 인한 cIAPs의 유비퀴틴 ligase 활성 조절

Authors 

Jin Sun ChoiByoung Chul ParkSeung-Wook ChiKwang-Hee BaeSun Hong KimS ChoW C SonP K MyungJeong Hoon KimSung Goo Park

Publisher 

Impact Journals

Issue Date 

2014

Citation 

Oncotarget, vol. 5, no. 20, pp. 10084-10099

Abstract 

HS-1-associated protein X-1 (HAX1) is a multi-functional protein which was first identified as a Hematopoietic cell specific Lyn Substrate 1 (HS1)-binding protein. Although the roles of HAX1 in apoptosis have been unraveled and HAX1 has been proposed to be involved in several diseases, additional roles of HAX1 are still being identified. Here, we demonstrated that HAX1 directly interacted with cellular Inhibitor of Apoptosis Proteins (cIAPs), ubiquitin E3 ligases which regulate the abundance of cellular proteins, via ubiquitin-dependent proteasomal degradation. We showed that HAX1 promotes auto-ubiquitination and degradation of cIAPs by facilitating the intermolecular homodimerization of RING finger domain. Moreover, HAX1 regulates the non-canonical Nuclear Factor-κB (NF-κB) signaling pathway by modulating the stability of NF-κB-Inducing Kinase (NIK), which is one of the substrates of cIAPs. Taken together, these results unveil a novel role of HAX1 in the non-canonical NF-κB pathway, and provide an important clue that HAX1 is a potential therapeutic target for the treatment of cancer.

ISSN 

1949-2553

Link 

http://dx.doi.org/10.18632/oncotarget.2459

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


Files in This Item: SizeFormat
12724.pdf4277KbAdobe PDF
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)