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Meeting Abstract

Structural Dynamics of the Rab5-Modulated Coiled-Coil Protein EEA1 Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry

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Lupas,  A       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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https://www.coiledcoils.net/download?name=Alpbach2017_program.pdf
(Abstract)

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Citation

Lauer, J., Lupas, A., & Zerial, M. (2017). Structural Dynamics of the Rab5-Modulated Coiled-Coil Protein EEA1 Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry. In 7th Alpbach Workshop: Coiled Coil, Fibrous and Repeat Proteins (pp. 39).


Cite as: https://hdl.handle.net/21.11116/0000-000B-6F09-0
Abstract
Intracellular trafficking of endosomes requires the cooperation of many soluble and membrane-bound components. The small GTPase Rab5 recruits a set of cytosolic effector molecules on the early endosome necessary for endosome biogenesis. Among them is the early endosome-associated autoantigen 1 (EEA1), whose homodimeric architecture consists of an N-terminal C2H2 Zn-finger followed by ~1200 residues of coiled coil, and a C-terminal FYVE domain. EEA1 binding to active Rab5, phosphatidylinositol 3-phosphate (PI3P), and syntaxins 6 and 13, helps regulate endosome tethering and fusion. This study utilized hydrogen deuterium exchange mass spectrometry (HDX-MS) to study the backbone dynamics of EEA1 and how they are regulated by Rab5 binding. Various mutants of EEA1 were generated to modulate coiled-coil stability. This produced valuable insights into how the fine-tuning of the coiled-coil structure controls binding events. We also found allosteric modulation of the coiled-coil structure upon binding Rab5 and noted that this allosteric modulation could be controlled by altering the stability of the coiled-coil.