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Role of GARP Vesicle Tethering Complex in Golgi Physiology

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Journal Int J Mol Sci
Publisher MDPI
Date 2023 Apr 13
PMID 37047041
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Abstract

The Golgi associated retrograde protein complex (GARP) is an evolutionarily conserved component of Golgi membrane trafficking machinery that belongs to the Complexes Associated with Tethering Containing Helical Rods (CATCHR) family. Like other multisubunit tethering complexes such as COG, Dsl1, and Exocyst, the GARP is believed to function by tethering and promoting fusion of the endosome-derived small trafficking intermediate. However, even twenty years after its discovery, the exact structure and the functions of GARP are still an enigma. Recent studies revealed novel roles for GARP in Golgi physiology and identified human patients with mutations in GARP subunits. In this review, we summarized our knowledge of the structure of the GARP complex, its protein partners, GARP functions related to Golgi physiology, as well as cellular defects associated with the dysfunction of GARP subunits.

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References
1.
Eising S, Thiele L, Frohlich F . A systematic approach to identify recycling endocytic cargo depending on the GARP complex. Elife. 2019; 8. PMC: 6374077. DOI: 10.7554/eLife.42837. View

2.
Frohlich F, Petit C, Kory N, Christiano R, Hannibal-Bach H, Graham M . The GARP complex is required for cellular sphingolipid homeostasis. Elife. 2015; 4. PMC: 4600884. DOI: 10.7554/eLife.08712. View

3.
Perez-Victoria F, Abascal-Palacios G, Tascon I, Kajava A, Magadan J, Pioro E . Structural basis for the wobbler mouse neurodegenerative disorder caused by mutation in the Vps54 subunit of the GARP complex. Proc Natl Acad Sci U S A. 2010; 107(29):12860-5. PMC: 2919957. DOI: 10.1073/pnas.1004756107. View

4.
Ibuchi K, Fukaya M, Shinohara T, Hara Y, Shiroshima T, Sugawara T . The Vps52 subunit of the GARP and EARP complexes is a novel Arf6-interacting protein that negatively regulates neurite outgrowth of hippocampal neurons. Brain Res. 2020; 1745:146905. DOI: 10.1016/j.brainres.2020.146905. View

5.
Conibear E, Stevens T . Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell. 2000; 11(1):305-23. PMC: 14776. DOI: 10.1091/mbc.11.1.305. View