title: The golgin tether giantin regulates the secretory pathway by controlling stack organization within Golgi apparatus.
abstract: Golgins are coiled-coil proteins that play a key role in the regulation of Golgi architecture and function. Giantin, the largest golgin in mammals, forms a complex with p115, rab1, GM130, and soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), thereby facilitating vesicle tethering and fusion processes around the Golgi apparatus. Treatment with the microtubule destabilizing drug nocodazole transforms the Golgi ribbon into individual Golgi stacks. Here we show that siRNA-mediated depletion of giantin resulted in more dispersed Golgi stacks after nocodazole treatment than by control treatment, without changing the average cisternal length. Furthermore, depletion of giantin caused an increase in cargo transport that was associated with altered cell surface protein glycosylation. Drosophila S2 cells are known to have dispersed Golgi stacks and no giantin homolog. The exogenous expression of mammalian giantin cDNA in S2 cells resulted in clustered Golgi stacks, similar to the Golgi ribbon in mammalian cells. These results suggest that the spatial organization of the Golgi ribbon is mediated by giantin, which also plays a role in cargo transport and sugar modifications.
authors.affiliation: The Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
authors.forename: Mayuko
authors.initials: M
authors.lastname: Koreishi
authors.forename: Thomas J
authors.initials: TJ
authors.lastname: Gniadek
authors.forename: Sidney
authors.initials: S
authors.lastname: Yu
authors.forename: Junko
authors.initials: J
authors.lastname: Masuda
authors.forename: Yasuko
authors.initials: Y
authors.lastname: Honjo
authors.forename: Ayano
authors.initials: A
authors.lastname: Satoh
mesh_terms: D000818:Animals; D001324:Autoantigens / Q000737:chemistry*; D002460:Cell Line; D002469:Cell Separation; D018076:DNA, Complementary / Q000378:metabolism; D004330:Drosophila; D005434:Flow Cytometry; D006031:Glycosylation; D006056:Golgi Apparatus / Q000378:metabolism*; D000077614:Golgi Matrix Proteins; D006367:HeLa Cells; D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry*; D015739:Nocodazole / Q000737:chemistry / Q000494:pharmacology*; D010641:Phenotype; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D050600:SNARE Proteins / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000378:metabolism
chemical_list: D001324:Autoantigens; D018076:DNA, Complementary; C028391:G protein, vesicular stomatitis virus; D000077614:Golgi Matrix Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D050600:SNARE Proteins; D014759:Viral Envelope Proteins; C087574:macrogolgin; D015739:Nocodazole
references.citation: J Cell Sci. 2002 Jul 1;115(Pt 13):2627-37
references.pmid: 12077354
references.citation: Traffic. 2003 Nov;4(11):739-53
references.pmid: 14617357
references.citation: Traffic. 2003 Mar;4(3):153-61
references.pmid: 12656988
references.citation: Traffic. 2007 Apr;8(4):339-46
references.pmid: 17319897
references.citation: Dev Cell. 2007 May;12(5):671-82
references.pmid: 17488620
references.citation: Science. 2008 Jun 20;320(5883):1651-4
references.pmid: 18566289
references.citation: Mol Membr Biol. 2003 Jul-Sep;20(3):209-20
references.pmid: 12893529
references.citation: Proc Natl Acad Sci U S A. 1995 May 23;92(11):5102-5
references.pmid: 7761455
references.citation: Histochem Cell Biol. 2008 Oct;130(4):709-17
references.pmid: 18648846
references.citation: Proc Natl Acad Sci U S A. 1976 Apr;73(4):1255-9
references.pmid: 1063406
references.citation: J Cell Biol. 2004 May 10;165(3):313-21
references.pmid: 15138289
references.citation: J Cell Biol. 1998 Mar 9;140(5):1013-21
references.pmid: 9490716
references.citation: J Cell Biol. 1995 Dec;131(6 Pt 2):1715-26
references.pmid: 8557739
references.citation: J Histochem Cytochem. 2005 Feb;53(2):249-52
references.pmid: 15684338
references.citation: Curr Opin Cell Biol. 2003 Aug;15(4):405-13
references.pmid: 12892780
references.citation: J Cell Biol. 2003 Jul 21;162(2):185-98
references.pmid: 12876273
references.citation: J Biol Chem. 2005 Jul 8;280(27):25840-8
references.pmid: 15878873
references.citation: Nature. 2000 Oct 26;407(6807):1022-6
references.pmid: 11069184
references.citation: J Biol Chem. 2001 Nov 30;276(48):45298-306
references.pmid: 11590181
references.citation: Exp Cell Res. 2007 Jul 1;313(11):2318-25
references.pmid: 17475246
references.citation: Science. 1996 Mar 15;271(5255):1526-33
references.pmid: 8599108
references.citation: Science. 2005 Feb 18;307(5712):1095-8
references.pmid: 15718469
references.citation: Nat Cell Biol. 2000 Nov;2(11):840-6
references.pmid: 11056540
references.citation: Protein Sci. 1996 Feb;5(2):185-94
references.pmid: 8745395
references.citation: J Biol Chem. 2000 Jan 28;275(4):2831-6
references.pmid: 10644749
references.citation: Annu Rev Cell Dev Biol. 2002;18:379-420
references.pmid: 12142281
references.citation: J Cell Sci. 2008 May 1;121(Pt 9):1538-46
references.pmid: 18411253
references.citation: FEBS Lett. 1997 Mar 17;405(1):107-10
references.pmid: 9094435
references.citation: Mol Biol Cell. 2009 Oct;20(19):4205-15
references.pmid: 19656848
references.citation: J Biol Chem. 2000 Apr 7;275(14):10196-201
references.pmid: 10744704
references.citation: Nat Cell Biol. 2001 Feb;3(2):140-9
references.pmid: 11175746
references.citation: Nat Cell Biol. 1999 May;1(1):E17-22
references.pmid: 10559876