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First published online August 9, 2006

Journal of Cell Science 119, 1605e (2006)
© The Company of Biologists Limited
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In this issue

A GRIPping tale of Golgi inheritance


Figure 1

How a new Golgi complex is produced when cells divide is an important problem in cell biology. Is a new one made from the ER or is the Golgi a unique organelle that duplicates through a template-based mechanism? And how general is the mechanism? On p. 3399, Robert Eisman, Thomas Kaufman and colleagues reveal that in Drosophila embryos a template-based mechanism is most likely and implicate the protein centrosomin's beautiful sister (Cbs) in the process. Peripheral membrane proteins called golgins, which often contain a conserved GRIP domain responsible for Golgi localization, have been implicated in Golgi inheritance in vertebrates. The authors report that Cbs also contains a GRIP domain and relocalizes from the cytoplasm to the chromosomes during late prometaphase in flies. This relocalization requires the Cbs GRIP domain and the ADP-ribosylation-factor-like GTPase Arl1. Moreover, it is essential for maintenance of the trans-Golgi complex during embryogenesis and centrosome maturation during mitosis. Thus, the embryonic Drosophila Golgi complex is more `vertebrate-like' than previously recognized, making Drosophila a good organism for future studies of Golgi inheritance.


Related articles in JCS:

centrosomin's beautiful sister (cbs) encodes a GRIP-domain protein that marks Golgi inheritance and functions in the centrosome cycle inDrosophila
Robert C. Eisman, Natasha Stewart, David Miller, and Thomas C. Kaufman
JCS 2006 119: 3399-3412. [Abstract] [Full Text]  




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