Results 71 to 80 of about 129,362 (255)
A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases
Ubiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible
Zuo-Xian Pu+9 more
doaj +1 more source
Quantitative proteomics identifies the Myb-binding protein p160 as a novel target of the von Hippel-Lindau tumor suppressor. [PDF]
The von Hippel-Lindau (VHL) tumor suppressor gene encodes a component of a ubiquitin ligase complex, which is best understood as a negative regulator of hypoxia inducible factor (HIF).
Yanlai Lai+4 more
doaj +1 more source
Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation [PDF]
The p53 tumor suppressor exerts anti-proliferative effects in response to various types of stress including DNA damage and abnormal proliferative signals. Tight regulation of p53 is essential for maintaining normal cell growth and this occurs primarily through posttranslational modifications of p53. Here, we describe Pirh2, a gene regulated by p53 that
Yunping Lin+11 more
openaire +4 more sources
The Role of the Cullin-5 E3 Ubiquitin Ligase in the Regulation of Insulin Receptor Substrate-1
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.
Christine Zhiwen Hu+2 more
doaj +1 more source
Reduced cul-5 activity causes aberrant follicular morphogenesis and germ cell loss in Drosophila oogenesis. [PDF]
Drosophila oogenesis is especially well suited for studying stem cell biology, cellular differentiation, and morphogenesis. The small modifier protein ubiquitin regulates many cellular pathways.
Jan-Michael Kugler+2 more
doaj +1 more source
The ubiquitin/26S proteasome pathway is a major route for degrading abnormal and important short-lived regulatory proteins in eukaryotes. Covalent attachment of ubiquitin, which triggers entry of target proteins into the pathway, is accomplished by an ...
Paul W. Bates, R. Vierstra
semanticscholar +1 more source
RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53
The RNF38 gene encodes a RING finger protein of unknown function. Here we demonstrate that RNF38 is a functional ubiquitin protein ligase (E3). We show that RNF38 isoform 1 is localized to the nucleus by a bipartite nuclear localization sequence (NLS). We confirm that RNF38 is a binding partner of p53 and demonstrate that RNF38 can ubiquitinate p53 in ...
C. Kenneth Kassenbrock+2 more
openaire +3 more sources
The protein substrate binding site of the ubiquitin-protein ligase system. [PDF]
In order to gain insight into the mechanisms that determine the selectivity of the ubiquitin proteolytic pathway, the protein substrate binding site of the ubiquitin-protein ligase system was identified and examined. Previous studies had shown that the ligase system consists of three components: a ubiquitin-activating enzyme (E1), ubiquitin-carrier ...
Hannah Heller+3 more
openaire +2 more sources
In vitro Auto- and Substrate-Ubiquitination Assays
The precise regulation of the homeostasis of the cellular proteome is critical for the appropriate growth and development of plants. It also allows the plants to respond to various environmental stresses, by modulating their biochemical and ...
Hye Park, Han Yong Lee, Gyeong Yoon
doaj +1 more source
In most instances, the transfer of ubiquitin to target proteins is catalyzed by the action of ubiquitin protein ligases (E3s). Full-length cDNAs encoding murine E6-associated protein (mE6-AP) as well as Nedd-4, a protein that is homologous to E6-AP in ...
S. Hatakeyama, J. P. Jensen, A. Weissman
semanticscholar +1 more source