Large ARF guanine nucleotide exchange factors in membrane trafficking (original) (raw)

Abstract.

In eukaryotic cells membrane compartments are connected through cargo-selective vesicle trafficking mediating the exchange of components between different organelles. This exchange is essential to maintain their structural integrity and specific composition. A fundamental regulatory step in vesicle formation is the activation of small ARF GTPases by exchanging their bound GDP for GTP, which is a prerequisite for ARF-mediated effector recruitment. Activation of ARFs is catalyzed by the characteristic SEC7 domain of guanine nucleotide exchange factors (ARF-GEFs), which are classified according to their additional protein domains.The only group of ARF-GEFs conserved in mammals, yeast and plants are the large ARF-GEFs. This review summarizes recent findings on the function of large ARF-GEFs, and the use of the inhibitor Brefeldin A as a potent tool in understanding membrane trafficking. Furthermore we highlight common themes and apparent differences in large ARF-GEF function between eukaryotic kingdoms.

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Authors and Affiliations

  1. Center of Molecular Biology of Plants, University of Tübingen, 72076, Tübingen, Germany
    N. Anders & G. Jürgens

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  1. N. Anders
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  2. G. Jürgens
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Correspondence toG. Jürgens.

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Received 25 April 2008; received after revision 26 May 2008; accepted 12 June 2008

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Anders, N., Jürgens, G. Large ARF guanine nucleotide exchange factors in membrane trafficking.Cell. Mol. Life Sci. 65, 3433–3445 (2008). https://doi.org/10.1007/s00018-008-8227-7

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