Picture of a black hole

Strathclyde Open Access research that creates ripples...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of research papers by University of Strathclyde researchers, including by Strathclyde physicists involved in observing gravitational waves and black hole mergers as part of the Laser Interferometer Gravitational-Wave Observatory (LIGO) - but also other internationally significant research from the Department of Physics. Discover why Strathclyde's physics research is making ripples...

Strathprints also exposes world leading research from the Faculties of Science, Engineering, Humanities & Social Sciences, and from the Strathclyde Business School.

Discover more...

The Ca2+-dependent lipid binding domain of P120(GAP) mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins : Evidence for a direct interaction between annexin VI and P120(GAP)

Davis, A J and Delafield-Butt, Jonathan and Walker, J H and Moss, S E and Gawler, D J (1996) The Ca2+-dependent lipid binding domain of P120(GAP) mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins : Evidence for a direct interaction between annexin VI and P120(GAP). Journal of Biological Chemistry, 271. pp. 24333-24336. ISSN 0021-9258

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

The CaLB domain is a 43-amino acid sequence motif found in a number of functionally diverse signaling proteins including three Ras-specific GTPase activating proteins (GAPs), In the Ras GTPase activating protein, p120(GAP), this domain has the ability to confer membrane association in response to intracellular Ca2+ elevation, Here we have isolated three proteins, p55, p70, and p120, which interact with the p120(GAP) CaLB domain in vitro. We identify p70 as the Ca2+-dependent phospholipid-binding protein annexin VI, Using co-immunoprecipitation studies, we have shown that the interaction between p120(GAP) and annexin VI is also detectable in rat fibroblasts, suggesting that this interaction may have a physiological role in vivo. Thus, the CaLB domain in p120(GAP) appears to have the ability to direct specific protein-protein interactions with Ca2+-dependent membrane-associated proteins, In addition, annexin VI is known to have tumor suppressor activity, Therefore, it is possible that the interaction of annexin VI with p120(GAP) may be important in the subsequent modulation of p21(ras) activity.