Specific auxin-binding proteins in the plasma membrane: receptors or transporters?

1992 ◽  
Vol 20 (1) ◽  
pp. 64-69 ◽  
Author(s):  
Terri L. Lomax ◽  
Glenn R. Hicks
1993 ◽  
Vol 340 (1293) ◽  
pp. 267-271 ◽  

Rho-related proteins are members of the ras superfamily of small GTP-binding proteins. Their function in fibroblasts has been analysed using microinjection of living cells. Rho appears to link plasma membrane receptors to the assembly of focal adhesions and actin stress fibres. The closely related protein rac, on the other hand, links receptors to the polymerization of actin at the plasma membrane to form membrane ruffles and pinocytotic vesicles. In phagocytic cells, rac has been shown to be required for activation of a membrane-bound NADPH oxidase in response to receptor activation. These systems provide the basis for a working model for the mechanism of action of the rho family of small GTPases.


Planta ◽  
1993 ◽  
Vol 189 (1) ◽  
Author(s):  
GlennR. Hicks ◽  
MargaretS. Rice ◽  
TerriL. Lomax

IUBMB Life ◽  
1997 ◽  
Vol 43 (4) ◽  
pp. 813-821
Author(s):  
Wojciech Szponarski ◽  
Jean-Benoît Peltier ◽  
Guillaume Tena ◽  
Michel Rossignol

Author(s):  
Elena Chiricozzi

AbstractPlasma membrane interaction is highly recognized as an essential step to start the intracellular events in response to extracellular stimuli. The ways in which these interactions take place are less clear and detailed. Over the last decade my research has focused on developing the understanding of the glycosphingolipids-protein interaction that occurs at cell surface. By using chemical synthesis and biochemical approaches we have characterized some fundamental interactions that are key events both in the immune response and in the maintenance of neuronal homeostasis. In particular, for the first time it has been demonstrated that a glycolipid, present on the outer side of the membrane, the long-chain lactosylceramide, is able to directly modulate a cytosolic protein. But the real conceptual change was the demonstration that the GM1 oligosaccharide chain is able, alone, to replicate numerous functions of GM1 ganglioside and to directly interact with plasma membrane receptors by activating specific cellular signaling. In this conceptual shift, the development and application of multidisciplinary techniques in the field of biochemistry, from chemical synthesis to bioinformatic analysis, as well as discussions with several national and international colleagues have played a key role.


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