Focal Hepatic 11C-Acetate Activity on PET/CT Scan Due to Lymphoid Hyperplasia

Huo, Li; Dang, Yongyan; Feng, Ruie; Lv, Jingqiao; Li, Fang

doi:10.1097/rlu.0000000000000634

Cited by 4 publications

(1 citation statement)

References 13 publications

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“…In addition to phosphorylation, ubiquitination, which involves the covalent attachment of ubiquitin to target proteins to regulate their half-lives, subcellular localization, activity and conformation, appears to be another important post-translational modification that helps fine-tune protein synthesis ( 20 ). Ubiquitination is a reversible process, and deubiquitinating enzymes (DUBs) cleave ubiquitin moieties from their substrates, to tightly control ubiquitination levels ( 21 ). It has been revealed that many ribosomal proteins, among both the small and large subunits ( 22 , 23 ), as well as several eIFs, including eIF5A ( 24 ), Paip1 ( 25 ), Paip2 ( 26 ), 4E-BP1 ( 27 ) and eIF2B epsilon ( 28 ) are ubiquitinated.…”

Section: Introductionmentioning

confidence: 99%

USP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1

Cheng

Chaerkady

et al. 2017

Nucleic Acids Research

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Controlling translation initiation is an efficient way to regulate gene expression at the post-transcriptional level. However, current knowledge regarding regulatory proteins and their modes of controlling translation initiation is still limited. In this study, we employed tandem affinity purification and mass spectrometry to screen for unknown proteins associated with the translation initiation machinery. Ubiquitin specific peptidase 9, X-linked (USP9X), was identified as a novel binding partner, that interacts with the eukaryotic translation initiation factor 4B (eIF4B) in a mRNA-independent manner. USP9X-deficient cells presented significantly impaired nascent protein synthesis, cap-dependent translation initiation and cellular proliferation. USP9X can selectively alter the translation of pro-oncogenic mRNAs, such as c-Myc and XIAP. Moreover, we found that eIF4A1, which is primarily ubiquitinated at Lys-369, is the substrate of USP9X. USP9X dysfunction increases the ubiquitination of eIF4A1 and enhances its degradation. Our results provide evidence that USP9X is a novel regulator of the translation initiation process via deubiquitination of eIF4A1, which offers new insight in understanding the pivotal role of USP9X in human malignancies and neurodevelopmental disorders.

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Section: Introductionmentioning

confidence: 99%

USP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1

Cheng

Chaerkady

et al. 2017

Nucleic Acids Research

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11C-Acetate PET/CT Monitoring Therapy of Multiple Myeloma

Zhu

Dang²,

Ma³

et al. 2016

Clinical Nuclear Medicine

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A 67-year-old man with newly diagnosed multiple myeloma underwent both FDG and C-acetate PET/CT sequentially on different days. There was increased FDG activity only in L1 vertebral body, but there was diffuse abnormal C-acetate activity throughout the skeletal system. After the successful therapy, the patient who was on remission clinically underwent follow-up PET/CT scans. Interestingly, L1 remained to have elevated FDG, although with less intensity. In contrast, there was no abnormal C-acetate activity anywhere in the body. The patient remained in remission clinically.

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