Regulation of GTP-binding state in RalA through Ca2+ and calmodulin

Experimental & Molecular Medicine
J B Park

Abstract

RalA GTPase, a member of Ras superfamily proteins, shows alternative forms between the active GTP-binding and the inactive GDP-binding states. Ral-specific guanine nucleotide exchange factor such as RalGDS interacts with activated Ras and cooperates with Ras indicating that Ral can be activated through Ras signaling pathway. Another activation path for Ral are through Ca2+-dependent but Ras-independent manner. In this study, studies were carried out to examine possible effects of Ca2+ and calmodulin, Ca2+-binding protein, directly on the GTP/GDP-binding state to recombinant unprenylated GST-RalA proteins. The results showed that Ca2+ stimulated the binding of GTP to RalA, whereas it reduced the binding of GDP to RalA. However, it does not involve a high affinity association of Ca2+ with RalA. Ca2+/calmodulin stimulated the GTPase activity of RalA. These results indicate that Ca2+ alone activates RalA by stimulating GTP-binding to RalA and Ca2+/calmodulin inactivates RalA by increasing the activity of RalGTPase.

Citations

May 3, 2003·Biochemical and Biophysical Research Communications·Ranjinder S SidhuRajinder P Bhullar
Feb 28, 2002·Molecular and Cellular Biology·Atsuko PolzinTimothy J Turner
Aug 30, 2005·Biochemical and Biophysical Research Communications·Ranjinder S SidhuRajinder P Bhullar
Mar 11, 2008·Biochimica Et Biophysica Acta·Sherif M Elsaraj, Rajinder P Bhullar
Dec 12, 2001·Nature Cell Biology·Serge MoskalenkoMichael A White
May 30, 2002·The Journal of Biological Chemistry·Richard R CloughRajinder P Bhullar
May 28, 2020·International Journal of Molecular Sciences·Francesc TebarThomas Grewal
Sep 5, 2021·Proceedings of the National Academy of Sciences of the United States of America·Samuel G ChamberlainHelen R Mott

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