An Enzyme Catalyzing O-Prenylation of the Glucose Moiety of Fusicoccin A, a Diterpene Glucoside Produced by the Fungus Phomopsis amygdali

ChemBioChem ◽  
2012 ◽  
Vol 13 (4) ◽  
pp. 566-573 ◽  
Author(s):  
Motoyoshi Noike ◽  
Chengwei Liu ◽  
Yusuke Ono ◽  
Yoshimitsu Hamano ◽  
Tomonobu Toyomasu ◽  
...  
Keyword(s):  
Fusicoccin A

Probing the 14-3-3 Isoform-Specificity Profile of Interactions Stabilized by Fusicoccin A

2020 ◽  
Author(s):  
James Frederich ◽  
Ananya Sengupta ◽  
Josue Liriano ◽  
Ewa A. Bienkiewicz ◽  
Brian G. Miller
Keyword(s):  
Protein Interactions ◽  
Neurological Diseases ◽  
Adapter Proteins ◽  
Protein Protein Interactions ◽  
Specific Expression ◽  
Individual Client ◽  
Isoform Specificity ◽  
Fusicoccin A

Fusicoccin A (FC) is a fungal phytotoxin that stabilizes protein–protein interactions (PPIs) between 14-3-3 adapter proteins and their phosphoprotein interaction partners. In recent years, FC has emerged as an important chemical probe of human 14-3-3 PPIs implicated in cancer and neurological diseases. These previous studies have established the structural requirements for FC-induced stabilization of 14-3-3·client phosphoprotein complexes; however, the effect of different 14-3-3 isoforms on FC activity has not been systematically explored. This is a relevant question for the continued development of FC variants because there are seven distinct isoforms of 14-3-3 in humans. Despite their remarkable sequence and structural similarities, a growing body of experimental evidence supports both tissue-specific expression of 14-3-3 isoforms and isoform-specific functions <i>in vivo</i>. Herein, we report the isoform-specificity profile of FC <i>in vitro</i>using recombinant human 14-3-3 isoforms and a focused library of fluorescein-labeled hexaphosphopeptides mimicking the C-terminal 14-3-3 recognition domains of client phosphoproteins targeted by FC in cell culture. Our results reveal modest isoform preferences for individual client phospholigands and demonstrate that FC differentially stabilizes PPIs involving 14-3-3s. Together, these data provide strong motivation for the development of non-natural FC variants with enhanced selectivity for individual 14-3-3 isoforms.

scholarly journals Probing the 14-3-3 Isoform-Specificity Profile of Interactions Stabilized by Fusicoccin A

2020 ◽  
Author(s):  
James Frederich ◽  
Ananya Sengupta ◽  
Josue Liriano ◽  
Ewa A. Bienkiewicz ◽  
Brian G. Miller
Keyword(s):  
Protein Interactions ◽  
Neurological Diseases ◽  
Adapter Proteins ◽  
Protein Protein Interactions ◽  
Specific Expression ◽  
Individual Client ◽  
Isoform Specificity ◽  
Fusicoccin A

Fusicoccin A (FC) is a fungal phytotoxin that stabilizes protein–protein interactions (PPIs) between 14-3-3 adapter proteins and their phosphoprotein interaction partners. In recent years, FC has emerged as an important chemical probe of human 14-3-3 PPIs implicated in cancer and neurological diseases. These previous studies have established the structural requirements for FC-induced stabilization of 14-3-3·client phosphoprotein complexes; however, the effect of different 14-3-3 isoforms on FC activity has not been systematically explored. This is a relevant question for the continued development of FC variants because there are seven distinct isoforms of 14-3-3 in humans. Despite their remarkable sequence and structural similarities, a growing body of experimental evidence supports both tissue-specific expression of 14-3-3 isoforms and isoform-specific functions <i>in vivo</i>. Herein, we report the isoform-specificity profile of FC <i>in vitro</i>using recombinant human 14-3-3 isoforms and a focused library of fluorescein-labeled hexaphosphopeptides mimicking the C-terminal 14-3-3 recognition domains of client phosphoproteins targeted by FC in cell culture. Our results reveal modest isoform preferences for individual client phospholigands and demonstrate that FC differentially stabilizes PPIs involving 14-3-3s. Together, these data provide strong motivation for the development of non-natural FC variants with enhanced selectivity for individual 14-3-3 isoforms.

Some effects of “fusicoccin A” on tomato leaf tissues

Life Sciences ◽  
1968 ◽  
Vol 7 (14) ◽  
pp. 751-760 ◽  
Author(s):  
A. Ballio ◽  
A. Graniti ◽  
F. Pocchiari ◽  
V. Silano
Keyword(s):  
Tomato Leaf ◽  
Leaf Tissues ◽  
Fusicoccin A

The phytotoxin fusicoccin, a selective stabilizer of 14-3-3 interactions?

IUBMB Life ◽  
2013 ◽  
Vol 65 (6) ◽  
pp. 513-517 ◽  
Author(s):  
Lorenzo Camoni ◽  
Sabina Visconti ◽  
Patrizia Aducci
Keyword(s):  
Fusicoccin A

scholarly journals Analysis of Interactions Stabilized by Fusicoccin A Reveals an Expanded Suite of Potential 14–3–3 Binding Partners

2020 ◽  
Vol 15 (2) ◽  
pp. 305-310 ◽  
Author(s):  
Ananya Sengupta ◽  
Josue Liriano ◽  
Brian G. Miller ◽  
James H. Frederich
Keyword(s):  
Binding Partners ◽  
Fusicoccin A

Probing the 14-3-3 Isoform-Specificity Profile of Interactions Stabilized by Fusicoccin A

2020 ◽  
Author(s):  
James Frederich ◽  
Ananya Sengupta ◽  
Josue Liriano ◽  
Ewa A. Bienkiewicz ◽  
Brian G. Miller
Keyword(s):  
Protein Interactions ◽  
Neurological Diseases ◽  
Adapter Proteins ◽  
Protein Protein Interactions ◽  
Specific Expression ◽  
Individual Client ◽  
Isoform Specificity ◽  
Fusicoccin A

Fusicoccin A (FC) is a fungal phytotoxin that stabilizes protein–protein interactions (PPIs) between 14-3-3 adapter proteins and their phosphoprotein interaction partners. In recent years, FC has emerged as an important chemical probe of human 14-3-3 PPIs implicated in cancer and neurological diseases. These previous studies have established the structural requirements for FC-induced stabilization of 14-3-3·client phosphoprotein complexes; however, the effect of different 14-3-3 isoforms on FC activity has not been systematically explored. This is a relevant question for the continued development of FC variants because there are seven distinct isoforms of 14-3-3 in humans. Despite their remarkable sequence and structural similarities, a growing body of experimental evidence supports both tissue-specific expression of 14-3-3 isoforms and isoform-specific functions <i>in vivo</i>. Herein, we report the isoform-specificity profile of FC <i>in vitro</i>using recombinant human 14-3-3 isoforms and a focused library of fluorescein-labeled hexaphosphopeptides mimicking the C-terminal 14-3-3 recognition domains of client phosphoproteins targeted by FC in cell culture. Our results reveal modest isoform preferences for individual client phospholigands and demonstrate that FC differentially stabilizes PPIs involving 14-3-3s. Together, these data provide strong motivation for the development of non-natural FC variants with enhanced selectivity for individual 14-3-3 isoforms.

Membrane Receptors for Fusicoccin: A Molecular Study

1992 ◽  
pp. 179-184 ◽  
Author(s):  
P. Aducci ◽  
A. Ballio ◽  
V. Fogliano ◽  
M. R. Fullone ◽  
M. Marra ◽  
...  
Keyword(s):  
Molecular Study ◽  
Membrane Receptors ◽  
Fusicoccin A

scholarly journals Fusicoccin: A Chemical Modulator for 14-3-3 Proteins

2021 ◽  
Vol 50 (1) ◽  
pp. 57-67
Author(s):  
Junko Ohkanda
Keyword(s):  
Fusicoccin A

ChemInform Abstract: KRISTALLSTRUKTUR VON FUSICOCCIN-A-P-JOD-BENZOLSULFONAT

1972 ◽  
Vol 3 (2) ◽  
Author(s):  
M. BRUFANI ◽  
S. CERRINI ◽  
W. FEDELI ◽  
A. VACIAGO
Keyword(s):  
Fusicoccin A

Fusicoccin-A selectively induces apoptosis in tumor cells after interferon-α priming

2010 ◽  
Vol 293 (2) ◽  
pp. 198-206 ◽  
Author(s):  
Ingrid J. de Vries-van Leeuwen ◽  
Chantal Kortekaas-Thijssen ◽  
Jean A. Nzigou Mandouckou ◽  
Sjors Kas ◽  
Antonio Evidente ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Interferon Α ◽  
Fusicoccin A
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