Proteomics and Biochemical Analyses of Secreted Proteins Revealed a Novel Mechanism by Which ADAM12S Regulates the Migration of Gastric Cancer Cells

Chang, Zenghui; Chen, Yu; Li, Dan; Jiang, Honglv; Ge, Fei; Xu, Guoqiang

doi:10.1021/acs.jproteome.2c00221

Cited by 4 publications

(2 citation statements)

References 53 publications

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“…The resulting tryptic peptides were extracted, vacuum-dried, resuspended in 0.1% trifluoroacetic acid, desalted with C18 ZipTips (Millipore, USA), vacuum-dried again, and dissolved in 0.1% formic acid. The peptide samples were analyzed in an Orbitrap Elite mass spectrometer as described previously …”

Section: Materials and Methodsmentioning

confidence: 99%

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Proximity Proteomics and Biochemical Analysis Reveal a Noncanonical Function for UFM1-Specific Protease 1 in the p62 Body Formation

et al. 2023

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Protein aggregates play crucial roles in the development of neurodegenerative diseases and p62 is one of the key proteins regulating the formation of protein aggregates. Recently, it has been discovered that depletion of several key enzymes including UFM1-activating enzyme UBA5, UFM1-conjugating enzyme UFC1, UFM1-protein ligase UFL1, and UFM1-specific protease UfSP2 in the UFM1-conjugation system induces p62 accumulation to form p62 bodies in the cytosol. However, it is unknown whether UfSP1 participates in the formation of p62 bodies and whether its enzymatic activity is required for this process. Here, the proximity labeling technique and quantitative proteomics identify SQSTM1/p62 as a UfSP1-interacting protein. Coimmunoprecipitation reveals that p62 indeed interacts with UfSP1 and the immunofluorescence experiment discloses that UfSP1 colocalizes with p62 and promotes the formation of p62-mediated protein aggregates. Mechanistic studies unveil that UfSP1 binds to the ubiquitin-associated domain of p62 and promotes the interaction between p62 and ubiquitinated proteins, thereby increasing the formation of p62 bodies. Interestingly, we further demonstrate that both the catalytic active and inactive UfSP1 promote the formation of p62 bodies through the same mechanism. Taken together, this work discovers that UfSP1 exhibits a noncanonical function independent of its protease activity in the p62 body formation.

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Section: Materials and Methodsmentioning

confidence: 99%

“…Raw proteomic data were searched using MaxQuant (Version 1.6.1.0) against a UniProt human protein database according to a procedure described previously. 36 Mass tolerances were set to 10 ppm for precursor ions and 0.6 Da for fragment ions, respectively. Cysteine carbamidomethylation was set as a fixed modification.…”

Section: Ms Data Analysismentioning

confidence: 99%