Forkhead box protein A2 (FOXA2) protein stability and activity are regulated by sumoylation. [PDF]
PLoS ONE, 2012 The forkhead box protein A2 (FOXA2) is an important regulator of glucose and lipid metabolism and organismal energy balance. Little is known about how FOXA2 protein expression and activity are regulated by post-translational modifications.
Narasimhaswamy S Belaguli +3 more
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PIAS Proteins Modulate Transcription Factors by Functioning as SUMO-1 Ligases [PDF]
Molecular and Cellular Biology, 2002 PIAS (protein inhibitor of activated STAT) proteins interact with and modulate the activities of various transcription factors. In this work, we demonstrate that PIAS proteins xalpha, xbeta, 1, and 3 interact with the small ubiquitin-related modifier SUMO-1 and its E2 conjugase, Ubc9, and that PIAS proteins themselves are covalently modified by SUMO-1 (
Noora, Kotaja +3 more
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Human immunodeficiency virus type 1 impairs sumoylation
Life Science Alliance, 2022 The HIV type 1 dampens host cell sumoylation in vitro and reduces the expression of UBA2 protein, a subunit of the SUMO E1–activating enzyme. In vivo, infection in patients is associated with diminished global leukocyte sumoylation activity.
Bilgül Mete +7 more
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SUMO-1 modification of centrosomal protein hNinein promotes hNinein nuclear localization [PDF]
Life Sciences, 2006 A centrosomal-associated protein, ninein is a microtubules minus end capping, centrosome position, and anchoring protein, but the underlying structure and physiological functions are still unknown. To identify the molecules that regulate the function of human ninein in centrosome, we performed yeast two-hybrid screen and isolated the SUMO-conjugating ...
Tai-Shan, Cheng +5 more
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SUMO-1 Controls the Protein Stability and the Biological Function of Phosducin [PDF]
GBM Fall meeting Hamburg 2007, 2006 Phosducin regulates Gbetagamma-stimulated signaling by binding to Gbetagamma subunits of heterotrimeric G-proteins. Control of phosducin activity by phosphorylation is well established. However, little is known about other mechanisms that may control phosducin activity.
Christoph, Klenk +3 more
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Analysis of SUMO-1 modification of neuronal proteins containing consensus SUMOylation motifs [PDF]
Neuroscience Letters, 2008 SUMOylation is emerging as an important mechanism for modulating protein function in many cell types. A large variety of proteins have been proposed as SUMO targets based on the presence of a consensus SUMOylation core motif (Psi-K-x-D/E). In neurons these include multiple synaptic proteins but it has not been established whether proteins carrying this
Wilkinson, KA, Nishimune, A, Henley, JM
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Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1 [PDF]
The EMBO Journal, 1999 The growth-suppressive properties of p53 are controlled by posttranslational modifications and by regulation of its turnover rate. Here we show that p53 can be modified in vitro and in vivo by conjugation to the small ubiquitin-like protein SUMO-1.
GOSTISSA M. +6 more
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Non-covalent Interaction With SUMO Enhances the Activity of Human Cytomegalovirus Protein IE1
Frontiers in Cell and Developmental Biology, 2021 Viruses interact with the host cellular pathways to optimize cellular conditions for replication. The Human Cytomegalovirus (HCMV) Immediate-Early protein 1 (IE1) is the first viral protein to express during infection.
Vasvi Tripathi +2 more
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Noncovalent SUMO-1 Binding Activity of Thymine DNA Glycosylase (TDG) Is Required for Its SUMO-1 Modification and Colocalization with the Promyelocytic Leukemia Protein [PDF]
Journal of Biological Chemistry, 2005 SUMO-1 is a member of a family of ubiquitin-like molecules that are post-translationally conjugated to various cellular proteins in a process that is mechanistically similar to ubiquitylation. To identify molecules that bind noncovalently to SUMO-1, we performed yeast two-hybrid screening with a SUMO-1 mutant that cannot be conjugated to target ...
Hidehisa, Takahashi +3 more
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Enhanced in vitro refolding of fibroblast growth factor 15 with the assistance of SUMO fusion partner. [PDF]
PLoS ONE, 2011 Fibroblast growth factor 15 (Fgf15) is the mouse orthologue of human FGF19. Fgf15 is highly expressed in the ileum and functions as an endocrine signal to regulate liver function, including bile acid synthesis, hepatocyte proliferation and insulin ...
Bo Kong, Grace L Guo
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