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First published online August 22, 2007


Journal of Cell Science 120, 1705e (2007)
© The Company of Biologists Limited
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In this issue

GAPs in Golgi formation


Figure 1

Rab GTPases control transport between the ER and the Golgi complex and, consequently, are important for maintenance of the Golgi. GTPase-activating proteins (GAPs) inactivate GTP-bound Rab proteins; so to discover which human Rab proteins are needed to maintain an active Golgi complex, Francis Barr and colleagues have screened a host of human Rab GAPs for the ability to disrupt the Golgi and ER-to-Golgi protein transport in human cells (see p. 2997). They find that only two GAPS (RN-tre and TBC1D20, GAPS for Rab43 and Rab1, respectively) disrupt both these processes. TBC1D20, the authors show, is localised to the ER by a transmembrane anchor and its overexpression blocks ER-to-Golgi transport and causes loss of the Golgi. Knocking down Rab1 by RNAi produces a similar phenotype, they report, whereas expression of the TBC1D20-binding partner reticulon antagonises the effects of TBC1D20 overexpression. The authors therefore conclude that Rab1 and Rab43 are required for the biogenesis and maintenance of human Golgi complexes.


Related articles in JCS:

Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
Alexander K. Haas, Shin-ichiro Yoshimura, David J. Stephens, Christian Preisinger, Evelyn Fuchs, and Francis A. Barr
JCS 2007 120: 2997-3010. [Abstract] [Full Text]  




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