Spectroscopic analysis of the interaction of rat liver short-chain, medium-chain, and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates

Biochemistry ◽  
1985 ◽  
Vol 24 (25) ◽  
pp. 7192-7199 ◽  
Author(s):  
Yasuyuki Ikeda ◽  
Kazuko Okamura-Ikeda ◽  
Kay Tanaka

1979 ◽  
Vol 98 (1) ◽  
pp. 165-172 ◽  
Author(s):  
Takao TANAKA ◽  
Kohei HOSAKA ◽  
Minoru HOSHIMARU ◽  
Shosaku NUMA




2002 ◽  
Vol 16 (5) ◽  
pp. 1049-1059 ◽  
Author(s):  
Hideki Katagiri ◽  
Tomoichiro Asano ◽  
Tetsuya Yamada ◽  
Toshifumi Aoyama ◽  
Yasushi Fukushima ◽  
...  

Abstract Insulin-regulated aminopeptidase (IRAP, also termed vp165) is known to be localized on the GLUT4-containing vesicles and to be recruited to the plasma membrane after stimulation with insulin. The cytoplasmic region of IRAP contains two dileucine motifs and acidic regions, one of which (amino acid residues 55–82) is reportedly involved in retention of GLUT4-containing vesicles. The region of IRAP fused with glutathione-S-transferase [GST-IRAP(55–82)] was incubated with lysates from 3T3-L1 adipocytes, leading to identification of long-chain, medium-chain, and short-chain acyl-coenzyme A dehydrogenases (ACDs) as the proteins associated with IRAP. The association was nearly abolished by mutation of the dileucine motif of IRAP. Immunoblotting of fractions prepared from sucrose gradient ultracentrifugation and vesicles immunopurified with anti-GLUT4 antibody revealed these ACDs to be localized on GLUT4-containing vesicles. Furthermore, 3-mercaptopropionic acid and hexanoyl-CoA, inhibitors of long-chain and medium-chain ACDs, respectively, induced dissociation of long-chain acyl-coenzyme A dehydrogenase and/or medium-chain acyl-coenzyme A dehydrogenase from IRAP in vitro as well as recruitment of GLUT4 to the plasma membrane and stimulation of glucose transport activity in permeabilized 3T3-L1 adipocytes. These findings suggest that ACDs are localized on GLUT4-containing vesicles via association with IRAP in a manner dependent on its dileucine motif and play a role in retention of GLUT4-containing vesicles to an intracellular compartment.



FEBS Letters ◽  
1979 ◽  
Vol 102 (2) ◽  
pp. 223-226 ◽  
Author(s):  
Jun-ichi Nikawa ◽  
Tadashi Tanabe ◽  
Hideo Ogiwara ◽  
Tetsuo Shiba ◽  
Shosaku Numa




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