RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53

Sheren, Jamie; Kassenbrock, C. Kenneth

doi:10.1016/j.bbrc.2013.08.031

Cited by 30 publications

(29 citation statements)

References 30 publications

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“…We show that Ub B directly simulates RING-independent and RING-dependent Ub transfer. Using the RING domain of RNF38, an E3 ligase implicated in p53 ubiquitination (Sheren and Kassenbrock, 2013), as a model system, we determine crystal structures of RNF38-RING bound to UbcH5B-Ub alone and in complex with free Ub bound to UbcH5B's backside. Comparison of the structures, together with other biophysical and biochemical analyses, reveals that Ub B alters UbcH5B dynamics and transforms RNF38-UbcH5B-Ub into a higher affinity complex with improved catalytic efficiency.…”

Section: Introductionmentioning

confidence: 99%

Activation of a Primed RING E3-E2–Ubiquitin Complex by Non-Covalent Ubiquitin

et al. 2015

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RING ubiquitin ligases (E3) recruit ubiquitin-conjugate enzymes (E2) charged with ubiquitin (Ub) to catalyze ubiquitination. Non-covalent Ub binding to the backside of certain E2s promotes processive polyUb formation, but the mechanism remains elusive. Here, we show that backside bound Ub (Ub(B)) enhances both RING-independent and RING-dependent UbcH5B-catalyzed donor Ub (Ub(D)) transfer, but with a more prominent effect in RING-dependent transfer. Ub(B) enhances RING E3s' affinities for UbcH5B-Ub, and RING E3-UbcH5B-Ub complex improves Ub(B)'s affinity for UbcH5B. A comparison of the crystal structures of a RING E3, RNF38, bound to UbcH5B-Ub in the absence and presence of Ub(B), together with molecular dynamics simulation and biochemical analyses, suggests Ub(B) restricts the flexibility of UbcH5B's α1 and α1β1 loop. Ub(B) supports E3 function by stabilizing the RING E3-UbcH5B-Ub complex, thereby improving the catalytic efficiency of Ub transfer. Thus, Ub(B) serves as an allosteric activator of RING E3-mediated Ub transfer.

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Section: Introductionmentioning

confidence: 99%

Activation of a Primed RING E3-E2–Ubiquitin Complex by Non-Covalent Ubiquitin

et al. 2015

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“…The proteins were then transferred to polyvinylidene difluoride membranes. The membranes were incubated in the following primary antibodies overnight at 4 °C (anti-NR1, 1:1000, #05–432 56 , Millipore, given by Yelin Chen lab; anti-GAPDH, 1:3000, Abmart, M20028 57 ). The membranes were then incubated in an anti-rabbit or anti-mouse secondary antibody conjugated to horseradish peroxidase (1:5000, TDYbio S001 and S004).…”

Section: Methodsmentioning

confidence: 99%

Mammillary body regulates state-dependent fear by alternating cortical oscillations

Jiang

Wang

Luo

et al. 2018

Sci Rep

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State-dependent memory describes a phenomenon that memory will be efficiently retrieved only when the brain state during retrieval matches the state during encoding. While a variety of psychoactive drugs, such as ethanol, cocaine, morphine and NMDA receptor antagonists, are able to induce state-dependent memory, the biological hallmark of brain state and neural mechanism of its regulation are still unknown. In this study, we found that MK-801 enhanced delta oscillations in awake mice, representing a drug-induced brain state, in which fear memory could only be successfully retrieved when the same drug condition was presented. We identified a key nucleus, mammillary body (MB), which regulates the specific brain state associated with MK-801. Chemogenetic silencing of MB neurons enhanced cortical delta oscillations and generated state-dependent memory. Moreover, optogenetic reconstitution of delta oscillations alone facilitated retrieval of fear memory encoded under MK-801. Our results indicated that delta oscillations in awake animals defined a specific brain state, in which memory formed is inaccessible under the normal condition, shining light on the neural mechanism underlying the fluctuation of memory retrieval and the role of MB in memory encoding and recall.

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“…Dysregulation of RNF38 is associated with a variety of diseases, including tumors. Furthermore, RNF38 has been reported to be a binding partner of p53 and induced the polyubiquitination of p53 in vitro and in vivo [4]. Furthermore, RNF38 has been reported to be a binding partner of p53 and induced the polyubiquitination of p53 in vitro and in vivo [4].…”

mentioning

confidence: 99%

“…In nonsmall cell lung cancer (NSCLC), RNF38 was elevated and this promoted the proliferation and metastatic capacity of NSCLC cells [3]. Furthermore, RNF38 has been reported to be a binding partner of p53 and induced the polyubiquitination of p53 in vitro and in vivo [4]. And overexpression of RNF38 resulted in relocalization of p53 to discrete foci associated with PML nuclear bodies [4].…”

mentioning

confidence: 99%

“…Furthermore, RNF38 has been reported to be a binding partner of p53 and induced the polyubiquitination of p53 in vitro and in vivo [4]. And overexpression of RNF38 resulted in relocalization of p53 to discrete foci associated with PML nuclear bodies [4]. Considering the extensive involvement of RNF38 in regulating p53 function, there is an urgent demand to identify the function and molecular mechanisms of RNF38 in gastric cancer.…”

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confidence: 99%

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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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RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53

Cited by 30 publications

References 30 publications

Activation of a Primed RING E3-E2–Ubiquitin Complex by Non-Covalent Ubiquitin

Activation of a Primed RING E3-E2–Ubiquitin Complex by Non-Covalent Ubiquitin

Mammillary body regulates state-dependent fear by alternating cortical oscillations

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

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