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J Cell Biol. 2001 Dec 10;155(6):873-5.
A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic.
Department of Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried D-82152, Germany.
Membrane traffic between the endoplasmic reticulum (ER) and Golgi apparatus and through the Golgi apparatus is a highly regulated process controlled by members of the rab GTPase family. The GTP form of rab1 regulates ER to Golgi transport by interaction with the vesicle tethering factor p115 and the cis-Golgi matrix protein GM130, also part of a complex with GRASP65 important for the organization of cis-Golgi cisternae. Here, we find that a novel coiled-coil protein golgin-45 interacts with the medial-Golgi matrix protein GRASP55 and the GTP form of rab2 but not other Golgi rab proteins. Depletion of golgin-45 disrupts the Golgi apparatus and causes a block in secretory protein transport. These results demonstrate that GRASP55 and golgin-45 form a rab2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure.
PMID: 11739401 [PubMed - indexed for MEDLINE]
PMCID: PMC2150909
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Cited by 14 PubMed Central articles
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Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins.
Sinka R, Gillingham AK, Kondylis V, Munro S.
J Cell Biol. 2008 Nov 17; 183(4):607-15. Epub 2008 Nov 10.
[J Cell Biol. 2008]
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Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi.
Hayes GL, Brown FC, Haas AK, Nottingham RM, Barr FA, Pfeffer SR.
Mol Biol Cell. 2009 Jan; 20(1):209-17. Epub 2008 Oct 22.
[Mol Biol Cell. 2009]
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The small GTPase Rab2 functions in the removal of apoptotic cells in Caenorhabditis elegans.
Mangahas PM, Yu X, Miller KG, Zhou Z.
J Cell Biol. 2008 Jan 28; 180(2):357-73.
[J Cell Biol. 2008]
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