Ubiquitination of the transcription factor c-MAF is mediated by multiple lysine residues

Chen, Guodong; Xu, Xin; Tong, Jiefei; Han, Kai; Zhang, Zubin; Tang, Juan; Li, Siyue; Yang, Chuanqi; Li, Jie; Cao, Biyin; Zhou, Haixia; Wu, Depei; Moran, Michael F.; Mao, Xinliang

doi:10.1016/j.biocel.2014.10.024

Cited by 29 publications

(48 citation statements)

References 33 publications

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“…Affinity purification-coupled mass spectrometry HEK293 cells were transfected with human c-Maf plasmid p-HA-c-Maf by using linear 25-Kd polyethyleimine (Sigma-Aldrich) 8 ; 24 hours later, cells were treated with 20 mM of MG132 for 2 hours and then solubilized in a lysis buffer containing BenzoNuclease (Novus). 12 After clarification by centrifugation and protein concentration determination, 10 mg of whole-cell lysates from each treatment were preincubated with protein A/G beads for 1 hour at 4°C, followed by incubation with anti-HA-conjugated agarose beads overnight at 4°C.…”

Section: Primary Bone Marrow Cellsmentioning

confidence: 99%

“…Luciferase activity was analyzed with the Bright-Glo substrate (Promega) as described previously. 8,9 Immunoblotting assay Immunoblotting (IB) assay was performed against specific antibodies as described previously.…”

Section: Luciferase-based Screenmentioning

confidence: 99%

“…Cell lysates were then prepared by using a lysis buffer containing 2% SDS, followed SDS-PAGE and IB analyses with specific antibodies. 8 …”

Section: Cycloheximide Chase Assaymentioning

confidence: 99%

“…7 Previous studies demonstrated that c-Maf protein stability is modulated by the ubiquitin-proteasome system. 8 c-Maf can be degraded in the proteasome after polyubiquitination, 4,9 which is mediated by 3 types of sequential enzymes, including ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). In humans there are 2 E1s, 35 known E2s, and ;300 to 600 E3s; these enzymes coordinately modulate ubiquitination of a vast diversity of substrate proteins.…”

Section: Introductionmentioning

confidence: 99%

“…The K to R c-Maf variants were generated by site-directed mutagenesis as reported previously. 8 MG132 was purchased from Sigma-Aldrich.…”

Section: Antibodies and Plasmidsmentioning

confidence: 99%

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The ubiquitin ligase HERC4 mediates c-Maf ubiquitination and delays the growth of multiple myeloma xenografts in nude mice

Zhang

Tong

Tang

et al. 2016

Blood

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Key Points• HERC4 is the first identified ubiquitin ligase that mediates c-Maf ubiquitination and degradation.• HERC4 suppresses MM cell proliferation and delays MM tumor growth.The transcription factor c-Maf is extensively involved in the pathophysiology of multiple myeloma (MM), a fatal malignancy of plasma cells. In the present study, affinity chromatography and mass spectrometry were used to identify c-Maf ubiquitination-associated proteins, from which the E3 ligase HERC4 was found to interact with c-Maf and catalyzed its polyubiquitination and subsequent proteasome-mediated degradation. HERC4 mediated polyubiquitination at K85 and K297 in c-Maf, and this polyubiquitination could be prevented by the isopeptidase USP5. Further analysis on the NCI-60 cell line collection revealed that RPMI 8226, a MM-derived cell line, expressed the lowest level of HERC4. Primary bone marrow analysis revealed HERC4 expression was high in normal bone marrow, but was steadily decreased during myelomagenesis. These findings suggested HERC4 played an important role in MM progression. Moreover, ectopic HERC4 expression decreased MM proliferation in vitro, and delayed xenograft tumor growth in vivo. Therefore, modulation of c-Maf ubiquitination by targeting HERC4 may represent a new therapeutic modality for MM. (Blood. 2016;127(13):1676-1686

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Section: Primary Bone Marrow Cellsmentioning

confidence: 99%

Section: Luciferase-based Screenmentioning

confidence: 99%

“…Cell lysates were then prepared by using a lysis buffer containing 2% SDS, followed SDS-PAGE and IB analyses with specific antibodies. 8 …”

Section: Cycloheximide Chase Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…The K to R c-Maf variants were generated by site-directed mutagenesis as reported previously. 8 MG132 was purchased from Sigma-Aldrich.…”

Section: Antibodies and Plasmidsmentioning

confidence: 99%

See 3 more Smart Citations

The ubiquitin ligase HERC4 mediates c-Maf ubiquitination and delays the growth of multiple myeloma xenografts in nude mice

Zhang

Tong

Tang

et al. 2016

Blood

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RING finger protein 38 induces gastric cancer cell growth by decreasing the stability of the protein tyrosine phosphatase SHP‐1

Zhang

et al. 2018

FEBS Letters

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The function of the E3 ligase RNF38 is still unknown in gastric cancer. Here, we found that RNF38 is upregulated in gastric cancer, and it is associated with the overall survival of gastric cancer patients. Further studies showed that RNF38 interacts with the nonreceptor tyrosine phosphatase SH2-containing protein tyrosine phosphatase 1 (SHP-1) and induces the polyubiquitination of SHP-1, which leads to destabilization of SHP-1 and promotion of STAT3 signaling in gastric cancer cells. In addition, overexpression or knockdown of RNF38 induces or suppresses gastric cancer cell growth in vitro, respectively, and silencing RNF38 delays tumor growth in vivo. These findings demonstrate that RNF38 is functional in gastric cancer and promotes STAT3 signaling by destabilizing SHP-1; thus, RNF38 could be a novel target for gastric cancer therapy.

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Ubiquitin specific peptidase 49 inhibits non‐small cell lung cancer cell growth by suppressing PI3K/AKT signaling

Shen

Yin

et al. 2019

The Kaohsiung J of Med Scie

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Ubiquitin specific peptidase 49 (USP49) has been reported as a tumor suppressor in several tumors, but its function and molecular mechanism in non‐small cell lung cancer (NSCLC) are still unknown. In this study, USP49 was found downregulated in NSCLC primary tissues and cell lines, and high USP49 predicted a positive index for the overall survival of NSCLC patients. Overexpression of USP49 downregulated the expression levels of Cyclin D1, and upregulated p53 expression. Further flow cytometry analysis showed that overexpressed USP49 induced cell cycle arrest at G0/G1 phase. As a result, overexpression of USP49 significantly inhibited cell growth of NSCLC cells. In mechanism, overexpression of USP49 inhibited PI3K/AKT signaling, but knockdown of USP49 enhanced this signaling. Further studies indicated that USP49 deubiquitinated PTEN and stabilized PTEN protein, which suggested that USP49 inhibited PI3K/AKT signaling by stabilizing PTEN in NSCLC cells. In conclusion, we demonstrated that USP49 was functional in NSCLC cells, and inhibited NSCLC cell growth by suppressing PI3K/AKT signaling, suggesting that USP49 could be as a novel target for NSCLC therapy.

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Ubiquitination of the transcription factor c-MAF is mediated by multiple lysine residues

Cited by 29 publications

References 33 publications

The ubiquitin ligase HERC4 mediates c-Maf ubiquitination and delays the growth of multiple myeloma xenografts in nude mice

The ubiquitin ligase HERC4 mediates c-Maf ubiquitination and delays the growth of multiple myeloma xenografts in nude mice

RING finger protein 38 induces gastric cancer cell growth by decreasing the stability of the protein tyrosine phosphatase SHP‐1

Ubiquitin specific peptidase 49 inhibits non‐small cell lung cancer cell growth by suppressing PI3K/AKT signaling

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