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About:
Site-Specific Photo-Crosslinking Proteomics Reveal Regulation of IFITM3 Trafficking and Turnover by VCP/p97 ATPase
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schema:ScholarlyArticle
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covidontheweb.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Site-Specific Photo-Crosslinking Proteomics Reveal Regulation of IFITM3 Trafficking and Turnover by VCP/p97 ATPase
Creator
Chandran, Kartik
Zhang, Yuqing
Peng, Tao
Das, Tandrila
Hang, Howard
Spence, Jennifer
Chen, Chengjie
Correspondence, Tao
Li, Yumeng
Sun, Yanan
Wu, Xiaojun
Yuan, Xiaoqiu
Source
Elsevier; Medline; PMC
abstract
Interferon-induced transmembrane protein 3 (IFITM3) is a key interferon effector that broadly prevents infection by diverse viruses. However, the cellular factors that control IFITM3 homeostasis and antiviral activity have not been fully elucidated. Using site-specific photo-crosslinking and quantitative proteomic analysis, here we present the identification and functional characterization of VCP/p97 AAA-ATPase as a primary interaction partner of IFITM3. We show that IFITM3 ubiquitination at lysine 24 is crucial for VCP binding, trafficking, turnover, and engagement with incoming virus particles. Consistently, pharmacological inhibition of VCP/p97 ATPase activity leads to defective IFITM3 lysosomal sorting, turnover, and co-trafficking with virus particles. Our results showcase the utility of site-specific protein photo-crosslinking in mammalian cells and reveal VCP/p97 as a key cellular factor involved in IFITM3 trafficking and homeostasis.
has issue date
2020-04-02
(
xsd:dateTime
)
bibo:doi
10.1016/j.chembiol.2020.03.004
bibo:pmid
32243810
has license
no-cc
sha1sum (hex)
b82a213e17b6e85dc534a8a4cccab82e7d15d067
schema:url
https://doi.org/10.1016/j.chembiol.2020.03.004
resource representing a document's title
Site-Specific Photo-Crosslinking Proteomics Reveal Regulation of IFITM3 Trafficking and Turnover by VCP/p97 ATPase
has PubMed Central identifier
PMC7194980
has PubMed identifier
32243810
schema:publication
Cell Chem Biol
resource representing a document's body
covid:b82a213e17b6e85dc534a8a4cccab82e7d15d067#body_text
is
schema:about
of
named entity 'Proteomics'
named entity 'ATPase'
named entity 'INTERACTING'
named entity 'PHOTO'
named entity 'ATPASE'
named entity 'SPECIFIC'
named entity 'leads'
named entity 'Highlights'
named entity 'turnover'
named entity 'Turnover'
named entity 'ATPase'
named entity 'ubiquitination'
named entity 'protein'
named entity 'IFITM3'
named entity 'Proteomics'
named entity 'VCP'
named entity 'p97'
named entity 'N-terminal'
named entity 'cycloalkene'
named entity 'Ifitm3'
named entity 'proximal'
named entity 'IAV'
named entity 'lysine'
named entity 'IFITM3'
named entity 'ubiquitinated'
named entity 'virus'
named entity 'plasmid'
named entity 'IFITM3'
named entity 'DMEM'
named entity 'live cells'
named entity 'ubiquitinated'
named entity 'IAV'
named entity '0.80'
named entity 'IFITM3'
named entity 'turnover rate'
named entity 'downregulation'
named entity 'HeLa'
named entity 'proteasome'
named entity 'innate immune response'
named entity 'crosslinking'
named entity 'crosslinking'
named entity 'lysosome'
named entity 'IFITM3'
named entity 'oligomers'
named entity 'mammalian cells'
named entity '0.01'
named entity 'antibody'
named entity 'IFITM3'
named entity 'Sigma-Aldrich'
named entity 'protein'
named entity 'virus replication'
named entity 'anti-Flag'
named entity 'cysteine'
named entity 'protein'
named entity 'unnatural amino acid'
named entity 'co-immunoprecipitated'
named entity 'alanine'
named entity 'IFITM3'
named entity 'steady state'
named entity 'Student's t test'
named entity 'covalent'
named entity 'Antiviral activity'
named entity 'IFITM3'
named entity 'stress conditions'
named entity 'Sigma-Aldrich'
named entity 'pharmacological'
named entity 'protein modification'
named entity 'crosslinked'
named entity 'IFITM3'
named entity 'IFITM3'
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