scholarly journals Multimeric Complexes among Ankyrin-Repeat and SOCS-box Protein 9 (ASB9), ElonginBC, and Cullin 5: Insights into the Structure and Assembly of ECS-type Cullin-RING E3 Ubiquitin Ligases

Biochemistry ◽  
2013 ◽  
Vol 52 (31) ◽  
pp. 5236-5246 ◽  
Author(s):  
Jemima C. Thomas ◽  
Dijana Matak-Vinkovic ◽  
Inge Van Molle ◽  
Alessio Ciulli
Keyword(s):  
Ubiquitin Ligases ◽  
Ankyrin Repeat ◽  
E3 Ubiquitin Ligases ◽  
Cullin 5 ◽  
Ring E3 ◽  
Socs Box

Cullin 5-RING E3 ubiquitin ligases, new therapeutic targets?

Biochimie ◽  
2016 ◽  
Vol 122 ◽  
pp. 339-347 ◽  
Author(s):  
Isabelle Lamsoul ◽  
Sandrine Uttenweiler-Joseph ◽  
Christel Moog-Lutz ◽  
Pierre G. Lutz
Keyword(s):  
Therapeutic Targets ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Cullin 5 ◽  
New Therapeutic Targets ◽  
Ring E3

scholarly journals TRIM32 and Malin in Neurological and Neuromuscular Rare Diseases

Cells ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 820
Author(s):  
Lorena Kumarasinghe ◽  
Lu Xiong ◽  
Maria Adelaida Garcia-Gimeno ◽  
Elisa Lazzari ◽  
Pascual Sanz ◽  
...  
Keyword(s):  
Common Ancestor ◽  
Genetic Diseases ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Lafora Disease ◽  
C Terminus ◽  
Rare Genetic Diseases ◽  
Tripartite Motif ◽  
Trim Proteins ◽  
Ring E3

Tripartite motif (TRIM) proteins are RING E3 ubiquitin ligases defined by a shared domain structure. Several of them are implicated in rare genetic diseases, and mutations in TRIM32 and TRIM-like malin are associated with Limb-Girdle Muscular Dystrophy R8 and Lafora disease, respectively. These two proteins are evolutionary related, share a common ancestor, and both display NHL repeats at their C-terminus. Here, we revmniew the function of these two related E3 ubiquitin ligases discussing their intrinsic and possible common pathophysiological pathways.

CRL3s: The BTB-CUL3-RING E3 Ubiquitin Ligases

2020 ◽  
pp. 211-223 ◽  
Author(s):  
Pu Wang ◽  
Junbin Song ◽  
Dan Ye
Keyword(s):  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Ring E3

scholarly journals Regulation of Cullin RING E3 Ubiquitin Ligases by CAND1 In Vivo

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16071 ◽  
Author(s):  
Yee Shin Chua ◽  
Boon Kim Boh ◽  
Wanpen Ponyeam ◽  
Thilo Hagen
Keyword(s):  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Ring E3

scholarly journals The Role of the Cullin-5 E3 Ubiquitin Ligase in the Regulation of Insulin Receptor Substrate-1

2012 ◽  
Vol 2012 ◽  
pp. 1-8
Author(s):  
Christine Zhiwen Hu ◽  
Jaswinder K. Sethi ◽  
Thilo Hagen
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Insulin Receptor ◽  
Ubiquitin Ligases ◽  
Insulin Receptor Substrate ◽  
E3 Ubiquitin Ligases ◽  
Kinase C ◽  
Cullin 5 ◽  
Socs Proteins ◽  
Protein Kinase C Activation

Background. SOCS proteins are known to negatively regulate insulin signaling by inhibiting insulin receptor substrate-1 (IRS1). IRS1 has been reported to be a substrate for ubiquitin-dependent proteasomal degradation. Given that SOCS proteins can function as substrate receptor subunits of Cullin-5 E3 ubiquitin ligases, we examined whether Cullin-5 dependent ubiquitination is involved in the regulation of basal IRS1 protein stability and signal-induced IRS1 degradation.Findings. Our results indicate that basal IRS1 stability varies between cell types. However, the Cullin-5 E3 ligase does not play a major role in mediating IRS1 ubiquitination under basal conditions. Protein kinase C activation triggered pronounced IRS1 destabilization. However, this effect was also independent of the function of Cullin-5 E3 ubiquitin ligases.Conclusions. In conclusion, SOCS proteins do not exert a negative regulatory effect on IRS1 by functioning as substrate receptors for Cullin-5-based E3 ubiquitin ligases both under basal conditions and when IRS1 degradation is induced by protein kinase C activation.

scholarly journals CRL4s: the CUL4-RING E3 ubiquitin ligases

2009 ◽  
Vol 34 (11) ◽  
pp. 562-570 ◽  
Author(s):  
Sarah Jackson ◽  
Yue Xiong
Keyword(s):  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Ring E3

scholarly journals Radiosensitization of Cancer Cells by Inactivation of Cullin-RING E3 Ubiquitin Ligases

2012 ◽  
Vol 5 (5) ◽  
pp. 305-312 ◽  
Author(s):  
Dongping Wei ◽  
Meredith A. Morgan ◽  
Yi Sun
Keyword(s):  
Cancer Cells ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Ring E3

scholarly journals Genome-Wide Identification of Grapevine's C3H2C3 Type RING E3 Ubiquitin Ligases Family Reveals VyRCHC114, which Confers Tolerance to Drought Stresses

2020 ◽  
Author(s):  
Yihe Yu ◽  
Shengdi Yang ◽  
Lu Bian ◽  
Keke Yu ◽  
Xiangxuan Meng ◽  
...  
Keyword(s):  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Genome Wide ◽  
Ring E3

scholarly journals Novel RING E3 Ubiquitin Ligases in Breast Cancer

Neoplasia ◽  
2006 ◽  
Vol 8 (8) ◽  
pp. 689-695 ◽  
Author(s):  
Angelika Burger ◽  
Yutaka Amemiya ◽  
Richard Kitching ◽  
Arun K. Seth
Keyword(s):  
Breast Cancer ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Ring E3
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