Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics-Reference-Cited by-同舟云学术

Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics

Published:2014-07-04 Issue:6192 Volume:345 Page:50-54
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Iversen Lars¹,Tu Hsiung-Lin¹,Lin Wan-Chen¹,Christensen Sune M.¹,Abel Steven M.²,Iwig Jeff³,Wu Hung-Jen¹,Gureasko Jodi³,Rhodes Christopher⁴,Petit Rebecca S.¹,Hansen Scott D.¹,Thill Peter⁵,Yu Cheng-Han⁶,Stamou Dimitrios⁷,Chakraborty Arup K.²⁵⁸⁹¹⁰,Kuriyan John¹³¹¹,Groves Jay T.¹⁶¹¹¹²

Affiliation:

1. Howard Hughes Medical Institute, Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.

2. Department of Chemical Engineering, Massachusetts Institute of Technology (MIT), Cambridge, MA 02139, USA.

3. Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.

4. Department of Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720, USA.

5. Department of Chemistry, MIT, Cambridge, MA 02139, USA.

6. Mechanobiology Institute, National University of Singapore, Singapore.

7. Department of Chemistry and Nano-Science Center, University of Copenhagen, Copenhagen, Denmark.

8. Department of Biological Engineering, MIT, Cambridge, MA 02139, USA.

9. Ragon Institute of Massachusetts General Hospital, MIT, and Harvard, Cambridge, MA 02139, USA.

10. Department of Physics, MIT, Cambridge, MA 02139, USA.

11. Physical Biosciences and Materials Sciences Divisions, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

12. Berkeley Education Alliance for Research in Singapore, 1 Create Way, CREATE tower level 11, University Town, Singapore 138602.

Abstract

Outliers dominate signaling at cell membrane SOS enzymes act at cell membranes to activate Ras, a regulatory protein often overactive in cancer cells. Iversen et al. devised a system where they could observe the activity of individual enzymes at work. The single SOS molecules occupied stable states that varied greatly in their catalytic activity. Regulation appeared to occur by altering the time spent in active states. The overall activity of SOS was determined by just a few molecules that achieved the highest catalytic activity. The methods described should allow further detailed kinetic analysis of this and other signaling events that occur at the cell membrane — properties that it is not possible to discern from bulk biochemical measurements. Science , this issue p. 50

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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