An endosomal tether undergoes an entropic collapse to bring vesicles together

A new endosomal tethering mechanism involving a mechanochemical cycle of the dimeric coiled-coil protein EEA1 regulated by Rab5:GTP binding and GTP hydrolysis. Flexible conformation for EEA1 tether protein Within cells, Rab GTPase proteins recruit tethering effectors that allow transport vesicles to...

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Veröffentlicht in:	Nature (London) 2016-09, Vol.537 (7618), p.107-111
Hauptverfasser:	Murray, David H., Jahnel, Marcus, Lauer, Janelle, Avellaneda, Mario J., Brouilly, Nicolas, Cezanne, Alice, Morales-Navarrete, Hernán, Perini, Enrico D., Ferguson, Charles, Lupas, Andrei N., Kalaidzidis, Yannis, Parton, Robert G., Grill, Stephan W., Zerial, Marino
Format:	Artikel
Sprache:	eng
Schlagworte:	14 14/19 14/28 14/35 631/45 631/57/2270 631/80/313/2011 631/80/313/2378 82 Allosteric Regulation Biological transport Cellular biology Endosomes - metabolism Entropy Guanosine Triphosphate - metabolism Humanities and Social Sciences Humans letter Membrane Fusion Membranes Microscopy multidisciplinary Optical Tweezers Phosphatidylinositol Phosphates - metabolism Pliability Protein Binding Protein Conformation Protein crosslinking Protein research Proteins rab5 GTP-Binding Proteins - metabolism Science SNARE Proteins - metabolism Structural analysis Vesicular Transport Proteins - chemistry Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism
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