Structure and Function of Transport Proteins That Form Solute Gradients

1999 ◽  
pp. 133-167
Author(s):  
Lon J. Van Winkle ◽  
Ovidio Bussolati ◽  
Gian Gazzola ◽  
John McGiven ◽  
Bryan Mackenzie ◽  
...  
2004 ◽  
Vol 21 (3) ◽  
pp. 171-181 ◽  
Author(s):  
Abraham B. Chang ◽  
Ron Lin ◽  
W. Keith Studley ◽  
Can V. Tran ◽  
Milton H. Saier, Jr

2002 ◽  
Vol 27 (5) ◽  
pp. 242-249 ◽  
Author(s):  
Liesbeth M Veenhoff ◽  
Esther H.M.L Heuberger ◽  
Bert Poolman

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Andrew J. Montalbano ◽  
Christopher S. Theisen ◽  
Eugene E. Fibuch ◽  
Norbert W. Seidler

GABAA receptor activity is directly modulated by glyceraldehyde 3-phosphate dehydrogenase (GAPDH), a protein with many nonglycolytic moonlighting functions. In addition to playing a role in the phosphorylation of the receptor, GAPDH may also participate in proper receptor trafficking to the plasma membrane. We previously showed that volatile anesthetics affect GAPDH structure and function that may contribute to the manner by which GAPDH modulates the GABAA receptor. In the current study, GAPDH interacted with engineered phospholipid-containing vesicles, preferring association with phosphatidylserine over phosphatidylcholine. Phosphatidyl-serine is known to participate in membrane trafficking of transport proteins and to play a role in GABAA receptor stability and function. We observed that GAPDH promoted the self-association and fusion of phosphatidyl-serine-rich vesicles as well as decreased membrane fluidity. Isoflurane enhanced each of these GAPDH-mediated events. Isoflurane also increased the binding of GAPDH to the cytoplasmic loop of the GABAA receptor. These observations are consistent with the working model of isoflurane playing a role in the trafficking of membrane proteins. This study is the first to implicate GAPDH and isoflurane in the regulation of GABAA receptor localization, providing insight into the mechanism of action of anesthesia.


2003 ◽  
Vol 48 (17) ◽  
pp. 1811-1815
Author(s):  
Chunling Yan ◽  
Min Lin ◽  
Yusong Wan ◽  
Shengqiang Hou ◽  
Shuzhen Ping ◽  
...  

Author(s):  
Peter Sterling

The synaptic connections in cat retina that link photoreceptors to ganglion cells have been analyzed quantitatively. Our approach has been to prepare serial, ultrathin sections and photograph en montage at low magnification (˜2000X) in the electron microscope. Six series, 100-300 sections long, have been prepared over the last decade. They derive from different cats but always from the same region of retina, about one degree from the center of the visual axis. The material has been analyzed by reconstructing adjacent neurons in each array and then identifying systematically the synaptic connections between arrays. Most reconstructions were done manually by tracing the outlines of processes in successive sections onto acetate sheets aligned on a cartoonist's jig. The tracings were then digitized, stacked by computer, and printed with the hidden lines removed. The results have provided rather than the usual one-dimensional account of pathways, a three-dimensional account of circuits. From this has emerged insight into the functional architecture.


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