ATP-binding Cassette (ABC) Transporter Supergene Family: Genetics and Evolution

Author(s):  
Michael Dean
2001 ◽  
Vol 42 (7) ◽  
pp. 1007-1017 ◽  
Author(s):  
Michael Dean ◽  
Yannick Hamon ◽  
Giovanna Chimini

2007 ◽  
Vol 282 (31) ◽  
pp. 22793-22803 ◽  
Author(s):  
Peter M. Jones ◽  
Anthony M. George

2019 ◽  
Vol 20 (13) ◽  
pp. 3178 ◽  
Author(s):  
Yu Ran Lee ◽  
Hee Kyoung Joo ◽  
Eun Ok Lee ◽  
Hyun Sil Cho ◽  
Sunga Choi ◽  
...  

Acetylation of nuclear apurinic/apyrimidinic endonuclease-1/redox factor-1 (APE1/Ref-1) is associated with its extracellular secretion, despite the lack of an N-terminal protein secretion signal. In this study, we investigated plasma membrane targeting and translocation of APE1/Ref-1 in HEK293T cells with enhanced acetylation. While APE1/Ref-1 targeting was not affected by inhibition of the endoplasmic reticulum/Golgi-dependent secretion, its secretion was reduced by inhibitors of ATP-binding cassette (ABC) transporters, and siRNA-mediated down-regulation of ABC transporter A1. The association between APE1/Ref-1 and ABCA1 transporter was confirmed by proximal ligation assay and immunoprecipitation experiments. An APE1/Ref-1 construct with mutated acetylation sites (K6/K7R) showed reduced co-localization with ABC transporter A1. Exposure of trichostatin A (TSA) induced the acetylation of APE1/Ref-1, which translocated into membrane fraction. Taken together, acetylation of APE1/Ref-1 is considered to be necessary for its extracellular targeting via non-classical secretory pathway using the ABCA1 transporter.


2011 ◽  
Vol 286 (43) ◽  
pp. 37280-37291 ◽  
Author(s):  
Akira Karasawa ◽  
Guus B. Erkens ◽  
Ronnie P.-A. Berntsson ◽  
Renee Otten ◽  
Gea K. Schuurman-Wolters ◽  
...  

1994 ◽  
Vol 13 (7) ◽  
pp. 1752-1759 ◽  
Author(s):  
K.M. Covitz ◽  
C.H. Panagiotidis ◽  
L.I. Hor ◽  
M. Reyes ◽  
N.A. Treptow ◽  
...  

2002 ◽  
Vol 15 (2) ◽  
pp. 102-108 ◽  
Author(s):  
André Fleiβner ◽  
Claudia Sopalla ◽  
Klaus-Michael Weltring

The necrotrophic pathogen Gibberella pulicaris infects potato tubers through wounds that contain fungitoxic secondary metabolites such as the phytoalexins rishitin and lubimin. In order to colonize tuber tissue, the fungus must possess a mechanism to tolerate potato defense compounds. In this paper, we show that a gene, Gpabc1, that codes an ATP-binding cassette (ABC) transporter is required for tolerance to these phytoalexins and for virulence on potato. The Gpabc1 gene, isolated in the course of a differential cDNA screen, shares high sequence homology with the ABC1 gene of Magnaporthe grisea. G. pulicaris mutants deficient in Gpabc1 were still able to metabolize rishitin but lost their tolerance to this phytoalexin as well as their virulence on potato. These results strongly suggest that the Gpabc1-encoded ABC transporter is necessary for tolerance of G. pulicaris to rishitin and that this tolerance is required for virulence on potato.


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