Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10803165 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2005 | 13 Pages |
Abstract
In this review we will focus on the recent advances in how coiled-coil proteins of the golgin family give identity and structure to the Golgi apparatus in animal cells. A number of recent studies reveal a common theme for the targeting of golgins containing the ARL-binding GRIP domain, and the related ARF-binding GRAB domain. Similarly, other golgins such as the vesicle tethering factor p115 and Bicaudal-D are targeted by the Rab GTPases, Rab1 and Rab6, respectively. Together golgins and their regulatory GTPases form a complex network, commonly known as the Golgi matrix, which organizes Golgi membranes and regulates membrane trafficking.
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Authors
Benjamin Short, Alexander Haas, Francis A. Barr,