An Alkyne–Aspirin Chemical Reporter for the Detection of Aspirin-Dependent Protein Modification in Living Cells

2013 ◽  
Vol 135 (39) ◽  
pp. 14568-14573 ◽  
Author(s):  
Leslie A. Bateman ◽  
Balyn W. Zaro ◽  
Stephanie M. Miller ◽  
Matthew R. Pratt
Keyword(s):  
Protein Modification ◽  
Living Cells ◽  
Chemical Reporter ◽  
Dependent Protein

scholarly journals Correction to “An Alkyne–Aspirin Chemical Reporter for the Detection of Aspirin-Dependent Protein Modification in Living Cells”

2018 ◽  
Vol 140 (14) ◽  
pp. 4954-4954
Author(s):  
Leslie A. Bateman ◽  
Balyn W. Zaro ◽  
Stephanie M. Miller ◽  
Matthew R. Pratt
Keyword(s):  
Protein Modification ◽  
Living Cells ◽  
Chemical Reporter ◽  
Dependent Protein

scholarly journals Monoclonal Antibodies to NTF2 Inhibit Nuclear Protein Import by Preventing Nuclear Translocation of the GTPase Ran

2000 ◽  
Vol 11 (2) ◽  
pp. 703-719 ◽  
Author(s):  
Susanne M. Steggerda ◽  
Ben E. Black ◽  
Bryce M. Paschal
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Import ◽  
Protein Import ◽  
Nuclear Translocation ◽  
Living Cells ◽  
Nuclear Accumulation ◽  
Nuclear Pore ◽  
Permeabilized Cells ◽  
Dependent Protein

Nuclear transport factor 2 (NTF2) is a soluble transport protein originally identified by its ability to stimulate nuclear localization signal (NLS)-dependent protein import in digitonin-permeabilized cells. NTF2 has been shown to bind nuclear pore complex proteins and the GDP form of Ran in vitro. Recently, it has been reported that NTF2 can stimulate the accumulation of Ran in digitonin-permeabilized cells. Evidence that NTF2 directly mediates Ran import or that NTF2 is required to maintain the nuclear concentration of Ran in living cells has not been obtained. Here we show that cytoplasmic injection of anti-NTF2 mAbs resulted in a dramatic relocalization of Ran to the cytoplasm. This provides the first evidence that NTF2 regulates the distribution of Ran in vivo. Moreover, anti-NTF2 mAbs inhibited nuclear import of both Ran and NLS-containing protein in vitro, suggesting that NTF2 stimulates NLS-dependent protein import by driving the nuclear accumulation of Ran. We also show that biotinylated NTF2-streptavidin microinjected into the cytoplasm accumulated at the nuclear envelope, indicating that NTF2 can target a binding partner to the nuclear pore complex. Taken together, our data show that NTF2 is an essential regulator of the Ran distribution in living cells and that NTF2-mediated Ran nuclear import is required for NLS-dependent protein import.

scholarly journals Dynamics of the distribution of cyclic AMP-dependent protein kinase in living cells.

1990 ◽  
Vol 87 (24) ◽  
pp. 9595-9599 ◽  
Author(s):  
J. L. Meinkoth ◽  
Y. Ji ◽  
S. S. Taylor ◽  
J. R. Feramisco
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Living Cells ◽  
Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals A bioorthogonal chemical reporter for fatty acid synthase-dependent protein acylation

2021 ◽  
pp. 101272
Author(s):  
Krithika P. Karthigeyan ◽  
Lizhi Zhang ◽  
David R. Loiselle ◽  
Timothy A.J. Haystead ◽  
Menakshi Bhat ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Chemical Reporter ◽  
Dependent Protein ◽  
Protein Acylation

scholarly journals The Metabolic Chemical Reporter Ac46AzGal Could Incorporate Intracellular Protein Modification in the Form of UDP-6AzGlc Mediated by OGT and Enzymes in the Leloir Pathway

2021 ◽  
Vol 9 ◽  
Author(s):  
Jiajia Wang ◽  
Biao Dou ◽  
Lu Zheng ◽  
Wei Cao ◽  
Peiyu Dong ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Protein Modification ◽  
Time Dependent ◽  
Dependent Manner ◽  
Intracellular Protein ◽  
Galactose Metabolism ◽  
Naturally Occurring ◽  
Leloir Pathway ◽  
Chemical Reporter ◽  
Complex Glycans

Galactose is a naturally occurring monosaccharide used to build complex glycans that has not been targeted for labeling as a metabolic reporter. Here, we characterize the cellular modification of proteins by using Ac46AzGal in a dose- and time-dependent manner. It is noted that a vast majority of this labeling of Ac46AzGal occurs intracellularly in a range of mammalian cells. We also provided evidence that this labeling is dependent on not only the enzymes of OGT responsible for O-GlcNAcylation but also the enzymes of GALT and GALE in the Leloir pathway. Notably, we discover that Ac46AzGal is not the direct substrate of OGT, and the labeling results may attribute to UDP-6AzGlc after epimerization of UDP-6AzGal via GALE. Together, these discoveries support the conclusion that Ac46AzGal as an analogue of galactose could metabolically label intracellular O-glycosylation modification, raising the possibility of characterization with impaired functions of the galactose metabolism in the Leloir pathway under certain conditions, such as galactosemias.

scholarly journals Protein modification characteristics of the malaria parasite Plasmodium falciparum and the infected erythrocytes

2020 ◽  
pp. mcp.RA120.002375
Author(s):  
Jianhua Wang ◽  
Ning Jiang ◽  
Xiaoyu Sang ◽  
Na Yang ◽  
Ying Feng ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Posttranslational Modifications ◽  
Protein Modification ◽  
Deep Understanding ◽  
Living Cells ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Dynamic Modification ◽  
Parasite Biology ◽  
Host Parasite

Malaria elimination is still pending on the development of novel tools that rely on a deep understanding of parasite biology. Proteins of all living cells undergo a myriad number of posttranslational modifications (PTMs) that are critical to multifarious life processes. An extensive proteome-wide dissection revealed a fine PTM map of most proteins in both Plasmodium falciparum, the causative agent of severe malaria, and the infected red blood cells. More than two-thirds of proteins of the parasite and its host cell underwent extensive and dynamic modification throughout the erythrocytic developmental stage. PTMs critically modulate the virulence factors involved in the host-parasite interaction and pathogenesis. Furthermore, P. falciparum stabilized the supporting proteins of erythrocyte origin by selective de-modification. Collectively, our multiple omic analyses, apart from having furthered a deep understanding of the systems biology of P. falciparum and malaria pathogenesis, provide a valuable resource for mining new antimalarial targets.

Glutathionylation of fibronectin records mechanical history, priming an integrin switch and myofibroblast polarization

2021 ◽  
Author(s):  
Wei Li ◽  
Leandro Moretti ◽  
Chiuan-Ren Yeh ◽  
Matthew Torres ◽  
Thomas Barker
Keyword(s):  
Conformational Changes ◽  
Posttranslational Modifications ◽  
Protein Modification ◽  
Polymer Network ◽  
Integrin Receptors ◽  
Post Translational Modifications ◽  
Cell Behaviors ◽  
Predominant Component ◽  
Physical Information ◽  
Dependent Protein

Abstract The extracellular matrix (ECM) is a protein polymer network that physically supports cells within a tissue and also acts as an important biochemical stimulus directing cell behaviors. For fibronectin, a predominant component of the ECM, these physical and biochemical activities are inextricably linked as physical forces trigger conformational changes that impact its biochemical activity. We analyzed whether oxidative post-translational modifications, specifically glutathionylation, enable fibronectin to ‘record’ physical information through stretch-dependent protein modification. Posttranslational modifications of the ECM are understudied, but represent opportunities for time- or stimuli-dependent changes in structure-function relationships that both persist over time and could have dominant impacts on cell-ECM homeostasis. We provide direct evidence that stretch-dependent glutathionylation of fibronectin irreversibly and significantly alters its mechanical properties with concomitant changes in the binding of integrin receptors and downstream cell signaling events. Stretch-dependent glutathionylation of fibronectin could have significant impact on the balance between tissue homeostasis and pathological progression, particularly in tissues and organs that are exposed to high oxidative stress, such as the lung.

Site-Specific Protein Modification on Living Cells Catalyzed by Sortase

ChemBioChem ◽  
2008 ◽  
Vol 9 (5) ◽  
pp. 802-807 ◽  
Author(s):  
Tsutomu Tanaka ◽  
Teruyasu Yamamoto ◽  
Shinya Tsukiji ◽  
Teruyuki Nagamune
Keyword(s):  
Protein Modification ◽  
Specific Protein ◽  
Living Cells ◽  
Site Specific
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