scholarly journals The Arabidopsis Mutant sleepy1gar2-1 Protein Promotes Plant Growth by Increasing the Affinity of the SCFSLY1 E3 Ubiquitin Ligase for DELLA Protein Substrates

2004 ◽  
Vol 16 (6) ◽  
pp. 1406-1418 ◽  
Author(s):  
Xiangdong Fu ◽  
Donald E. Richards ◽  
Barbara Fleck ◽  
Daoxin Xie ◽  
Nicolas Burton ◽  
...  
Keyword(s):  
Plant Growth ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Della Protein ◽  
Protein Substrates ◽  
Arabidopsis Mutant

scholarly journals A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates

2018 ◽  
Vol 294 (7) ◽  
pp. 2470-2485 ◽  
Author(s):  
Cyrus Tan ◽  
Eamon F. X. Byrne ◽  
Casey Ah-Cann ◽  
Melissa J. Call ◽  
Matthew E. Call
Keyword(s):  
Ubiquitin Ligase ◽  
Transmembrane Domain ◽  
E3 Ubiquitin Ligase ◽  
Down Regulation ◽  
Protein Substrates

Parkin: a multifaceted ubiquitin ligase

2006 ◽  
Vol 34 (5) ◽  
pp. 749-753 ◽  
Author(s):  
D.J. Moore
Keyword(s):  
Ubiquitin Ligase ◽  
Dopaminergic Neurons ◽  
Autosomal Recessive ◽  
E3 Ubiquitin Ligase ◽  
Gene Products ◽  
Biochemical Pathway ◽  
Leucine Rich Repeat ◽  
Parkin Gene ◽  
Protein Substrates ◽  
Phosphatase And Tensin Homologue

Mutations in the parkin gene are a common cause of autosomal recessive early-onset parkinsonism. Parkin functions as an E3 ubiquitin ligase where it can polyubiquitinate a number of its protein substrates, thus targeting them for degradation by the 26 S proteasomal complex. Recent studies have demonstrated that alternative modes of parkin-mediated ubiquitination may serve other non-degradative regulatory roles. In addition, parkin appears to function as a multipurpose neuroprotectant in a number of toxic paradigms. Coupled with these observations, parkin may integrate other gene products associated with parkinsonism, including α-synuclein, LRRK2 (leucine-rich repeat kinase 2), DJ-1 and PINK1 [PTEN (phosphatase and tensin homologue deleted on chromosome 10)-induced putative kinase 1], into a common biochemical pathway of potential relevance to disease pathogenesis. Parkin therefore represents a unique multifaceted ubiquitin ligase consistent with an important housekeeping role in maintaining the integrity or survival of dopaminergic neurons.

scholarly journals Illuminating the COP1/SPA Ubiquitin Ligase: Fresh Insights Into Its Structure and Functions During Plant Photomorphogenesis

2021 ◽  
Vol 12 ◽  
Author(s):  
Jathish Ponnu ◽  
Ute Hoecker
Keyword(s):  
Arabidopsis Thaliana ◽  
Plant Growth ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Growth Development ◽  
Structure And Functions ◽  
Spa Proteins

CONSTITUTIVE PHOTOMORPHOGENIC 1 functions as an E3 ubiquitin ligase in plants and animals. Discovered originally in Arabidopsis thaliana, COP1 acts in a complex with SPA proteins as a central repressor of light-mediated responses in plants. By ubiquitinating and promoting the degradation of several substrates, COP1/SPA regulates many aspects of plant growth, development and metabolism. In contrast to plants, human COP1 acts as a crucial regulator of tumorigenesis. In this review, we discuss the recent important findings in COP1/SPA research including a brief comparison between COP1 activity in plants and humans.

Author response for "TAM receptors attenuate murine NK cell responses via E3 ubiquitin ligase Cbl‐b"

2019 ◽  
Author(s):  
Leilani M. Chirino ◽  
Suresh Kumar ◽  
Mariko Okumura ◽  
David E. Sterner ◽  
Michael Mattern ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Nk Cell ◽  
E3 Ubiquitin Ligase ◽  
Author Response ◽  
Cell Responses ◽  
Tam Receptors
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