Functional involvement of TMF/ARA160 in Rab6-dependent retrograde membrane traffic

Experimental Cell Research

Volumn 313, Issue 16, 2007, Pages 3472-3485

  Yamane, Junko ^a,b   Kubo, Akiharu ^b,c   Nakayama, Kazuhisa ^a   Yuba Kubo, Akiko ^d   Katsuno, Tatsuya ^e   Tsukita, Shoichiro ^a,b   Tsukita, Sachiko ^b,e  

^a KYOTO UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c KEIO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^d MITSUBISHI KAGAKU INSTITUTE OF LIFE SCIENCES   (Japan)

^e OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

Glycosyltransferase; Golgi; Rab6; Retrograde transport; Shiga toxin; TMF ARA160

Indexed keywords

ACYLTRANSFERASE; BETA 1,4 GALACTOSYLTRANSFERASE; GALACTOSYLTRANSFERASE; N ACETYLGALACTOSAMINYLTRANSFERASE 2; PROTEIN DERIVATIVE; RAB PROTEIN; RAB6 PROTEIN; SHIGA TOXIN; TATA ELEMENT MODULATORY FACTOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENDOSOME; GOLGI COMPLEX; HUMAN; HUMAN CELL; IMMUNOELECTRON MICROSCOPY; IMMUNOFLUORESCENCE; LYSOSOME; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; RNA INTERFERENCE;

EID: 34548646335     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.07.010     Document Type: Article

References (60)

1. Sannerud R., Saraste J., and Goud B. Retrograde traffic in the biosynthetic-secretory route: pathways and machinery. Curr. Opin. Cell Biol. 15 (2003) 438-445
2. Lee M.C., Miller E.A., Goldberg J., Orci L., and Schekman R. Bi-directional protein transport between the ER and Golgi. Annu. Rev. Cell Dev. Biol. 20 (2004) 87-123
3. Storrie B. Maintenance of Golgi apparatus structure in the face of continuous protein recycling to the endoplasmic reticulum: making ends meet. Int. Rev. Cyt. 244 (2005) 69-94
4. Storrie B., White J., Röttger S., Stelzer E.H., Suganuma T., and Nilsson T. Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143 (1998) 1505-1521
5. Girod A., Storrie B., Simpson J.C., Johannes L., Goud B., Roberts L.M., Lord J.M., Nilsson T., and Pepperkok R. Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum. Nat. Cell Biol. 1 (1999) 423-430
6. White J., Johannes L., Mallard F., Girod A., Grill S., Reinsch S., Keller P., Tzschaschel B., Echard A., Goud B., and Stelzer H.K. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J. Cell Biol. 147 (1999) 743-760
7. Mallard F., Antony C., Tenza D., Salamero J., Goud B., and Johannes L. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport. J. Cell Biol. 143 (1998) 973-990
8. Chavrier P., and Goud B. The role of ARF and Rab GTPases in membrane transport. Curr. Opin. Cell Biol. 11 (1999) 466-475
9. Zerial M., and McBride H. Rab proteins as membrane organizers. Nat. Rev., Mol. Cell Biol. 2 (2001) 107-117
10. Pfeffer S., and Aivazian D. Targeting Rab GTPases to distinct membrane compartments. Nat. Rev., Mol. Cell Biol. 5 (2004) 886-896
11. Seabra M.C., and Wasmeier C. Controlling the location and activation of Rab GTPases. Curr. Opin. Cell Biol. 16 (2004) 451-457
12. Grosshans B.L., Ortiz D., and Novick P. Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 11821-11827
13. Echard A., Opdam F.J., de Leeuw H.J., Jollivet F., Savelkoul P., Hendriks W., Voorberg J., Goud B., and Fransen J.A. Alternative splicing of the human Rab6A gene generates two close but functionally different isoforms. Mol. Biol. Cell 11 (2000) 3819-3833
14. Opdam F.J., Echard A., Croes H.J., van den Hurk J.A., van de Vorstenbosch R.A., Ginsel L.A., Goud B., and Fransen J.A. The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus. J. Cell Sci. 113 (2000) 2725-2735
15. Martinez O., Antony C., Pehau-Arnaudet G., Berger E.G., Salamero J., and Goud B. GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 1828-1833
16. Mallard F., Tang B.L., Galli T., Tenza D., Saint-Pol A., Yue X., Antony C., Hong W., Goud B., and Johannes L. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 56 (2002) 653-664
17. Monier S., Jollivet F., Janoueix-Lerosey I., Johannes L., and Goud B. Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport. Traffic 3 (2002) 289-297
18. Young J., Stauber T., del Nery E., Vernos I., Pepperkok R., and Nilsson T. Regulation of microtubule-dependent Recycling at the TGN by Rab6A and Rab6A′. Mol. Biol. Cell 16 (2005) 162-177
19. Del Nery E., Miserey-Lenkei S., Falguieres T., Nizak C., Johannes L., Perez F., and Goud B. Rab6A and Rab6A′ GTPases play non-overlapping roles in membrane trafficking. Traffic 7 (2006) 394-407
20. Utskarpen A., Slagsvold H.H., Iversen T.G., Walchli S., and Sandvig K. Transport of ricin from endosome to the Golgi apparatus is regulated by Rab6A and Rab6A′. Traffic 7 (2006) 663-672
21. Nakagawa Y., Yamane Y., Okanoue T., Tsukita S., and Tsukita S. Outer dense fiber 2 is a widespread centrosome scaffold component preferentially associated with mother centrioles: its identification from isolated centrosomes. Mol. Biol. Cell 12 (2001) 1687-1697
22. Garcia J.A., Ou S.H., Wu F., Lusis A.J., Sparkes R.S., and Gaynor R.B. Cloning and chromosomal mapping of a human immunodeficiency virus 1 "TATA" element modulatory factor. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 9372-9376
23. Hsiao P.W., and Chang C. Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells. J. Biol. Chem. 274 (1999) 22373-22379
24. Mori K., and Kato H. A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2 α and BRG-1/hSNF2 β and localizes in the Golgi apparatus. FEBS Lett. 520 (2002) 127-132
25. Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., and Nir U. TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3. Oncogene 23 (2004) 8908-8919
26. Fridmann-Sirkis Y., Siniossoglou S., and Pelham H.R. TMF is a golgin that binds Rab6 and influences Golgi morphology. BMC Cell Biol. 5 (2004) 18
27. Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., and Shiina N. Centriolar satellites: molecular characterization, ATP-dependent movement toward centrioles and possible involvement in ciliogenesis. J. Cell Biol. 147 (1999) 969-980
28. Nakamura N., Rabouille C., Watson R., Nilsson T., Hui N., Slusarewicz P., Kreis T.E., and Warren G. Characterization of a cis-Golgi matrix protein, GM130. J. Cell Biol. 31 (1995) 1715-1726
29. Yoshimura S., Yamamoto A., Misumi Y., Sohda M., Barr F.A., Fujii G., Shakoori A., Ohno H., Mihara K., and Nakamura N. Dynamics of Golgi matrix proteins after the blockage of ER to Golgi transport. J. Biochem. (Tokyo) 135 (2004) 201-216
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
31. Niwa H., Yamamura K., and Miyazaki J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108 (1991) 193-199
32. Shin H.W., Shinotsuka C., Torii S., Murakami K., and Nakayama K. Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J. Biochem. (Tokyo) 122 (1997) 525-530
33. Miyake M., Utsuno E., and Noda M. Binding of avian ovomucoid to shiga-like toxin type 1 and its utilization for receptor analog affinity chromatography. Anal. Biochem. 281 (2000) 202-208
34. Shin H.W., Morinaga N., Noda M., and Nakayama K. BIG2, a guanine nucleotide exchange factor for ADP-ribosylation factors: its localization to recycling endosomes and implication in the endosome integrity. Mol. Biol. Cell 15 (2004) 5283-5294
35. Shin H.W., Kobayashi H., Kitamura M., Waguri S., Suganuma T., Uchiyama Y., and Nakayama K. Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking. J. Cell Sci. 118 (2005) 4039-4048
36. Stefanini M., De Martino C., and Zamboni I. Fixation of ejaculated spermatozoa for electron microscopy. Nature 216 (1967) 173-174
37. Fujiwara T., Oda K., Yokota S., Takatsuki A., and Ikehara Y. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263 (1988) 18545-18552
38. Klausner R.D., Donaldson J.G., and Lippincott-Schwartz J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116 (1992) 1071-1080
39. Jiang S., and Storrie B. Cisternal Rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress. Mol. Biol. Cell 16 (2005) 2586-2596
40. Short B., Haas A., and Barr F.A. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim. Biophys. Acta 1744 (2005) 383-395
41. Fujiwara T., Misumi Y., and Ikehara Y. Dynamic recycling of ERGIC53 between the endoplasmic reticulum and the Golgi complex is disrupted by nordihydroguaiaretic acid. Biochem. Biophys. Res. Commun. 253 (1998) 869-876
42. Yoshino A., Setty S.R., Poynton C., Whiteman E.L., Saint-Pol A., Burd C.G., Johannes L., Holzbaur E.L., Koval M., McCaffery J.M., and Marks M.S. tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing center. J. Cell Sci. 18 (2005) 2279-2293
43. Graham T.R. Membrane targeting: getting Arl to the Golgi. Curr. Biol. 14 (2004) R483-R485
44. Munro S. Sequences within and adjacent to the transmembrane segment of α-2,6-sialyltransferase specify Golgi retention. EMBO J. 10 (1991) 3577-3588
45. Nilsson T., Lucocq J.M., Mackay D., and Warren G. The membrane spanning domain of β-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10 (1991) 3567-3575
46. Dahdal R.Y., and Colley K.J. Specific sequences in the signal anchor of the β-galactoside α-2,6-sialyltransferase are not essential for Golgi localization. Membrane flanking sequences may specify Golgi retention. J. Biol. Chem. 268 (1993) 26310-26319
47. Lussier M., Sdicu A.M., Ketela T., and Bussey H. Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p α-1,2-mannosyltransferase to a medial-Golgi compartment. J. Cell Biol. 131 (1995) 913-927
48. Colley K.J. Golgi localization of glycosyltransferases: more questions than answers. Glycobiology 7 (1997) 1-13
49. Andersson A.M., and Pettersson R.F. Targeting of a short peptide derived from the cytoplasmic tail of the G1 membrane glycoprotein of Uukuniemi virus (Bunyaviridae) to the Golgi complex. J. Virol. 72 (1998) 9585-9596
50. Gonatas J.O., Chen Y.J., Stieber A., Mourelatos Z., and Gonatas N.K. Truncations of the C-terminal cytoplasmic domain of MG160, a medial Golgi sialoglycoprotein, result in its partial transport to the plasma membrane and filopodia. J. Cell Sci. 111 (1998) 249-260
51. Milland J., Taylor S.G., Dodson H.C., McKenzie I.F., and Sandrin M.S. The cytoplasmic tail of α1,2-fucosyltransferase contains a sequence for Golgi localization. J. Biol. Chem. 276 (2001) 12012-12018
52. Milland J., Russell S.M., Dodson H.C., McKenzie I.F., and Sandrin M.S. The cytoplasmic tail of α1,3-galactosyltransferase inhibits Golgi localization of the full-length enzyme. J. Biol. Chem. 277 (2002) 10374-10378
53. Glick B.S. Can the Golgi form de novo?. Nat. Rev., Mol. Cell Biol. 3 (2002) 615-619
54. Mironov A.A., Beznoussenko G.V., Polishchuk R.S., and Trucco A. Intra-Golgi transport: a way to a new paradigm?. Biochim. Biophys. Acta 1744 (2005) 340-350
55. Losev E., Reinke C.A., Jellen J., Strongin D.E., Bevis B.J., and Glick B.S. Golgi maturation visualized in living yeast. Nature 441 (2006) 1002-1006
56. Matsuura-Tokita K., Takeuchi M., Ichihara A., Mikuriya K., and Nakano A. Live imaging of yeast Golgi cisternal maturation. Nature 41 (2006) 1007-1010
57. Malhotra V., and Mayor S. Cell biology: the Golgi grows up. Nature 441 (2006) 939-940
58. Röttger S., White J., Wandall H.H., Olivo J.C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., and Nilsson T. Localization of three human polypeptide GalNac-transferase in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J. Cell Sci. 111 (1998) 45-60
59. Uliana A.S., Giraudo C.G., and Maccioni H.J. Cytoplasmic tails of SialT2 and GalNAcT impose their respective proximal and distal Golgi localization. Traffic 7 (2006) 604-612
60. Schaub B.E., Berger B., Berger E.G., and Rohrer J. Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated. Mol. Biol. Cell 17 (2006) 5153-5162