Golgins and GTPases, giving identity and structure to the Golgi apparatus.
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.
Intracellular Protein Transport, Independent Junior Research Group, Max-Planck-Institute of Biochemistry, Martinsried, 82152, Germany.
Benjamin
B
Short
Alexander
A
Haas
Francis A
FA
Barr
D000818:Animals; D017209:Apoptosis / Q000502:physiology; D003599:Cytoskeleton / Q000378:metabolism; D006056:Golgi Apparatus / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008938:Mitosis / Q000502:physiology; D020691:rab GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*
D008565:Membrane Proteins; D020691:rab GTP-Binding Proteins