scholarly journals Role of the F‐box protein exchange factor in the reproductive growth of Arabidopsis

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Melaku Garsamo ◽  
Lihong Li ◽  
Yun Zhou ◽  
Xing Liu
Neuroreport ◽  
2003 ◽  
Vol 14 (5) ◽  
pp. 759-761 ◽  
Author(s):  
Youyi Dong ◽  
Takayuki Nakagawa ◽  
Tsuyoshi Endo ◽  
Tae-Soo Kim ◽  
Fukuichiro Iguchi ◽  
...  

1980 ◽  
Vol 48 (2) ◽  
pp. 273-280 ◽  
Author(s):  
H. van der Zee ◽  
A. B. Malik ◽  
B. C. Lee ◽  
T. S. Hakim

2013 ◽  
Vol 144 (5) ◽  
pp. S-314
Author(s):  
Stefanie Zenker ◽  
Stefan J. Wirtz ◽  
Tadamitsu Kishimoto ◽  
Maximilian J. Waldner ◽  
Markus F. Neurath ◽  
...  

2003 ◽  
Vol 2 (1) ◽  
pp. 123-133 ◽  
Author(s):  
Cheryl Dixon ◽  
Lee Ellen Brunson ◽  
Mary Margaret Roy ◽  
Dechelle Smothers ◽  
Michael G. Sehorn ◽  
...  

ABSTRACT Ubiquitin ligases direct the transfer of ubiquitin onto substrate proteins and thus target the substrate for proteasome-dependent degradation. SCF complexes are a family of ubiquitin ligases composed of a common core of components and a variable component called an F-box protein that defines substrate specificity. Distinct SCF complexes, defined by a particular F-box protein, target different substrate proteins for degradation. Although a few have been identified to be involved in important biological pathways, such as the cell division cycle and coordinating cellular responses to changes in environmental conditions, the role of the overwhelming majority of F-box proteins is not clear. Creating inhibitors that will block the in vivo activities of specific SCF ubiquitin ligases may provide identification of substrates of these uncharacterized F-box proteins. Using Saccharomyces cerevisiae as a model system, we demonstrate that overproduction of polypeptides corresponding to the amino terminus of the F-box proteins Cdc4p and Met30p results in specific inhibition of their SCF complexes. Analyses of mutant amino-terminal alleles demonstrate that the interaction of these polypeptides with their full-length counterparts is an important step in the inhibitory process. These results suggest a common means to inhibit specific SCF complexes in vivo.


2017 ◽  
Vol 28 (13) ◽  
pp. 1768-1781 ◽  
Author(s):  
Alejandra Valdivia ◽  
Silvia M. Goicoechea ◽  
Sahezeel Awadia ◽  
Ashtyn Zinn ◽  
Rafael Garcia-Mata

Circular dorsal ruffles (CDRs) are actin-rich structures that form on the dorsal surface of many mammalian cells in response to growth factor stimulation. CDRs represent a unique type of structure that forms transiently and only once upon stimulation. The formation of CDRs involves a drastic rearrangement of the cytoskeleton, which is regulated by the Rho family of GTPases. So far, only Rac1 has been consistently associated with CDR formation, whereas the role of other GTPases in this process is either lacking or inconclusive. Here we show that RhoG and its exchange factor, Trio, play a role in the regulation of CDR dynamics, particularly by modulating their size. RhoG is activated by Trio downstream of PDGF in a PI3K- and Src-dependent manner. Silencing RhoG expression decreases the number of cells that form CDRs, as well as the area of the CDRs. The regulation of CDR area by RhoG is independent of Rac1 function. In addition, our results show the RhoG plays a role in the cellular functions associated with CDR formation, including macropinocytosis, receptor internalization, and cell migration. Taken together, our results reveal a novel role for RhoG in the regulation of CDRs and the cellular processes associated with their formation.


2012 ◽  
Vol 7 (1) ◽  
pp. 50-52
Author(s):  
Nobuhiro Tanaka ◽  
Jun-Ichi Itoh ◽  
Yasuo Nagato

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