Nuclear Translocation of a Key Regulator of Glycolysis: 6-phosphofructo-2-kinase (pfkfb3)

نویسندگان

  • Abdullah Yalcin
  • Brian F. Clem
  • Alan Simmons
  • Andrew Lane
  • Kristin Nelson
  • Amy L. Clem
  • Erin Brock
  • Deanna Siow
  • Binks Wattenberg
  • Sucheta Telang
  • Jason Chesney
  • James Graham Brown
چکیده

PROLIFERATION VIA CYCLIN-DEPENDENT KINASES Abdullah Yalcin, Brian F. Clem, Alan Simmons, Andrew Lane, Kristin Nelson, Amy L. Clem, Erin Brock, Deanna Siow, Binks Wattenberg, Sucheta Telang and Jason Chesney Division of Medical Oncology (Molecular Targets Group), James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202 Department of Biochemistry, School of Veterinary Medicine, Uludag University, Bursa, Turkey. Running Head: Nuclear 6-Phosphofructo-2-Kinase (PFKFB3) Activity Address Correspondence to: Jason Chesney, MD PhD, Division of Medical Oncology, James Graham Brown Cancer Center, University of Louisville, 580 South Preston Street, #204E, Louisville, Kentucky 40202, Tel. 502 852-3402; Fax 502 852-3661; E-Mail: [email protected]

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6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase) catalyzes the synthesis and degradation of fructose 2,6-bisphosphate (F2,6BP), which is a powerful activator of 6-phosphofructo-1-kinase, the rate-limiting enzyme of glycolysis. Four genes encode PFK-2/FBPase (PFKFB1-4), and an inducible isoform (iPFK-2/PFKFB3) has been found to mediate F2,6BP production in proliferating cells....

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تاریخ انتشار 2009