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GTPase and ATPase tangos during intracellular protein targeting

Shan, Shu-ou (2013) GTPase and ATPase tangos during intracellular protein targeting. FASEB Journal, 27 . Art. No. 198.1. ISSN 0892-6638.

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Rougly one third of the proteome are destined for the cellular membrane, whose proper localization is essential for the structure and function of all cells. The signal recognition particle (SRP) is a universally conserved cellular machinery that couples the synthesis of membrane and secretory proteins to their proper cellular localization, and has served as a paradigm to understand the molecular basis of protein localization. Using a combination of chemical, biophysical, structural and cellular approaches, our work has established a quantitative framework for how two highly homologous GTPases in the SRP and SRP receptor use a novel GTPase cycle to drive this fundamental cellular pathway, and elucidated how fidelity of protein localization by the SRP is achieved through a combination of binding, induced fit, and kinetic proofreading mechanisms. These findings also define a novel class of ‘dimerization-activated’ GTPases, represented by the SRP and SRP receptor, whose regulatory principles may extend to a growing number of nucleotide hydrolases that drive diverse cellular processes.

Item Type:Article
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Shan, Shu-ou0000-0002-6526-1733
Additional Information:© 2013 FASEB.
Record Number:CaltechAUTHORS:20130711-133855161
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:39321
Deposited By: Tony Diaz
Deposited On:17 Jul 2013 22:18
Last Modified:03 Oct 2019 05:06

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