Evidence map›Paper›PMID 40198702›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.

Ya-Ting Zhong, Li-Li Huang, Kangning Li, Bingke Yang, Xueting Ye, Hao-Ran Zhong, Bing Yu, Menghan Ma, Yuerong Yuan, Yang Meng and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

17 authors.

Ya-Ting Zhong *Guangdong Provincial Clinical Research Center for Cancer, State Key Laboratory of Oncology in South China, Sun Yat-sen University Cancer Center, Guangzhou, Guangdong 510060, China.
Li-Li Huang *Guangdong Provincial Clinical Research Center for Cancer, State Key Laboratory of Oncology in South China, Sun Yat-sen University Cancer Center, Guangzhou, Guangdong 510060, China.
Kangning Li *State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin 300071, China.
Bingke YangState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin 300071, China.
Xueting YeDepartment of Chemistry and Research Center for Chemical Biology and Omics Analysis, College of Science, Southern University of Science and Technology, Shenzhen 518055, China.
Hao-Ran ZhongGuangdong Provincial Clinical Research Center for Cancer, State Key Laboratory of Oncology in South China, Sun Yat-sen University Cancer Center, Guangzhou, Guangdong 510060, China.
Bing YuGuangdong Provincial Clinical Research Center for Cancer, State Key Laboratory of Oncology in South China, Sun Yat-sen University Cancer Center, Guangzhou, Guangdong 510060, China.
Menghan MaState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin 300071, China.
Yuerong YuanCollege of Life Sciences, Nankai University, Tianjin 300071, China.
Yang MengCollege of Life Sciences, Nankai University, Tianjin 300071, China.
Runfeng PanCollege of Life Sciences, Nankai University, Tianjin 300071, China.
Haiqing ZhangCollege of Life Sciences, Nankai University, Tianjin 300071, China.ORCID 0009-0006-3631-1902
Lijun ShiState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin 300071, China.ORCID 0009-0000-9947-8810
Yunyun WangState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin 300071, China.
Ruijun TianDepartment of Chemistry and Research Center for Chemical Biology and Omics Analysis, College of Science, Southern University of Science and Technology, Shenzhen 518055, China.ORCID 0000-0001-9521-5124
Song GaoGuangdong Provincial Clinical Research Center for Cancer, State Key Laboratory of Oncology in South China, Sun Yat-sen University Cancer Center, Guangzhou, Guangdong 510060, China.
Xin BianState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin 300071, China.ORCID 0000-0002-5501-0471

Funding

MOST | National Key Research and Development Program of China (NKPs) 2018YFA0508300MOST | National Natural Science Foundation of China (NSFC) 22125403MOST | National Natural Science Foundation of China (NSFC) 32320103002MOST | National Natural Science Foundation of China (NSFC) 32371287MOST | National Natural Science Foundation of China (NSFC) 82173098MOST | National Natural Science Foundation of China (NSFC) 92253304
6 · The paper itself

Abstract

Most members of the dynamin superfamily of large guanosine triphophatases (GTPases) have an ability to remodel membranes in response to guanosine triphosphate (GTP) hydrolysis. Ring Finger Protein 112 (RNF112) (ZNF179/neurolastin) is a recently identified brain-specific dynamin-like protein possessing a really interesting new gene (RING) finger domain. Despite its essential role as an E3 ligase in neuron development, the architecture of RNF112 and the exact role of its GTPase activity remain unknown. Here, we determined the crystal structure of truncated RNF112 (RNF112

Indexed as

BrainDynaminsAnimalsCrystallography, X-RayGTP PhosphohydrolasesGuanosine TriphosphateHumansHydrolysisModels, MolecularProtein DomainsUbiquitin-Protein LigasesDynaminsGTP PhosphohydrolasesGuanosine TriphosphateUbiquitin-Protein Ligasesdynamin superfamilymembrane remodelingprotein structure

Identifiers

PMID40198702
PMCPMC12012479

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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.