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Section: Figures
Postdoctoral
Position
Available

Lab Page Link

Anthony Carruthers, Ph.D.

Academic Role: Professor

Faculty Appointment(s) In:
   Biochemistry and Molecular Pharmacology
   Physiology

Other Affiliation(s):
   Center for AIDS Research
   Graduate School of Biomedical Sciences

Figures

Ultrastructure of Human Erythrocyte GLUT1

Ultrastructure of Human Erythrocyte GLUT1

Analysis of GLUT1 aggregation state by freeze-fracture electron microscopy. High magnification of unidirectionally shadowed freeze-fractured electron micrographs of GLUT1 proteoliposomes. Composite of nonreduced (left) and reduced (middle), purified GLUT1 Integral Membrane Particles. The bar represents 10 nm. The images represent the average of 60 particles. The rightmost image shows the dimensions of monomeric GLUT1 threaded through GlpT structure.

Structural basis of GLUT1 regulation by ATP

Structural basis of GLUT1 regulation by ATP

ATP regulation of GLUT1. GLUT1 membrane spanning topography is illustrated. GLUT1 behavior is illustrated in the presence of AMP (left) or ATP (right). Trypsin cleavage sites (yellow and brown circles), sites of antibody recognition (green and red sequence), and sites where IgG binding is not detected (blue sequence) are indicated. In the presence of ATP (right), ATP-sensitive (red sequence) and insensitive (green sequence) IgG binding domains are also indicated. The circles show ATP-insensitive tryptic cleavage sites (yellow circles), ATP-protected tryptic cleavage sites (brown circles), and ATP-protected sites of lysine covalent modification by Sulfo-NHS-LC-Biotin (red circles). We propose that the GLUT1 C-terminus and the C-terminal half of the middle loop interact in response to ATP binding. This reduces their respective accessibility to polar reagents and restricts glucose release from the translocation pathway.


Office: S1-842B
Phone: 508-856-6074 & 5570
Fax: 508-856-3659 or 508-856-6464
E-mail: Anthony.Carruthers@umassmed.edu
Keywords: Biophysics, Cell Biology, Biochemistry, Structural Biology

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Postdoctoral Position Available

A postdoctoral position is available in this laboratory to study sugar transporter biology.

 Contact Dr. Anthony Carruthers for more details.

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