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A Novel Cytosolic GTP-Binding Protein with Phospholipid Stimulated GTP-Binding And GTPase Activity

  • Ronit Sagi-Eisenberg
  • Linton M. Traub
  • Galia Gat-Yablonski
  • Meir Aridor

Abstract

The signal transducing GTP-binding proteins (G-proteins) isolated thus far are membrane associated. However, rapidly accumulating data suggest that regulatory G-proteins may also be cytosolic. This conclusion is based mainly on indirect observations such as the ability of cytosol to restore adenylate cyclase activity of cyc- membranes (1), the presence of cholera or pertussis toxins substrates in the cytosol (2,3) and the activation of a soluble phosphoirositide-hydrolyzing PLC by GTP-ɣ-S (4). The firadings that the purified α-subunits of Go and Gi are water soluble (5), that oc-subunits of Gs are released from the membrane following activation (6) and that about 80% of the GTP-binding protein ARF is located in the cytosolic fraction (7) further support his notion. Indeed, it has been recently argued that the critical interactions of the signal transducing G-proteins occur in the cytoplasm rather than in the membrane (8). In addition, several reports (9–11) have implicated GTP-binding proteins as regulatory elements in the transport and secretion of proteins. These data again imply that the distribution and function of G-proteins should be extended from the surface of the cell to the interior (12).

Keywords

Cytosolic Fraction Guanine Nucleotide Diphteria Toxin Pertussis Toxin Substrate Binding Polypeptide Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Ronit Sagi-Eisenberg
    • 1
  • Linton M. Traub
    • 1
  • Galia Gat-Yablonski
    • 1
  • Meir Aridor
    • 1
  1. 1.Department of Chemical ImmunologyThe Weizmann Institute of ScienceRehovotIsrael

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