Evidence map›Paper›PMID 25275296›Full record

ArticleOncotarget2014

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

Jin Sun Choi, Byoung Chul Park, Seung Wook Chi, Kwang-Hee Bae, Sunhong Kim, Sayeon Cho, Woo-Chan Son, Pyung Keun Myung, Jeong-Hoon Kim, Sung Goo Park

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 42% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 11 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 1 country.

Jin Sun ChoiMedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea. College of Pharmacy, Chungnam National University, Daejeon, Republic of Korea.
Byoung Chul ParkMedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea.
Seung Wook ChiMedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea.
Kwang-Hee BaeCell Function Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea.
Sunhong KimTargeted Medicine Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea. Department of Biomolecular Science, University of Science and Technology (UST), Daejeon, Republic of Korea.
Sayeon ChoCollege of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.
Woo-Chan SonAsan Institute for Life Sciences and Asan Medical Center, Seoul, Republic of Korea. Department of Pathology, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea.
Pyung Keun MyungCollege of Pharmacy, Chungnam National University, Daejeon, Republic of Korea.
Jeong-Hoon KimTargeted Gene Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea. Department of Functional Genomics, Daejeon, Republic of Korea.
Sung Goo ParkMedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea.
Korea Research Institute of Bioscience and Biotechnology · KRChung-Ang University · KRChungnam National University · KRUlsan College · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Adaptor Proteins, Signal TransducingApoptosisBaculoviral IAP Repeat-Containing 3 ProteinCell Line, TumorHEK293 CellsHumansInhibitor of Apoptosis ProteinsNF-kappa BNF-kappaB-Inducing KinaseProtein MultimerizationProtein Serine-Threonine KinasesSignal TransductionTransfectionUbiquitinationUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingBaculoviral IAP Repeat-Containing 3 ProteinBIRC3 protein, humanHAX1 protein, humanInhibitor of Apoptosis ProteinsNF-kappa BNF-kappaB-Inducing KinaseProtein Serine-Threonine KinasesUbiquitin-Protein Ligases

Identifiers

PMID25275296
PMCPMC4259407
OpenAlexW1938197645

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.