메뉴 건너뛰기




Volumn 15, Issue 4, 2013, Pages 417-429

PtdIns(4)P regulates retromer-motor interaction to facilitate dynein-cargo dissociation at the trans-Golgi network

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; P150 PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHOTIDYLINOSITOL 4 PHOSPHATE; SNX1 PROTEIN; SNX6 PROTEIN; UNCLASSIFIED DRUG;

EID: 84876479440     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2710     Document Type: Article
Times cited : (56)

References (49)
  • 6
    • 0035965256 scopus 로고    scopus 로고
    • βiII spectrin binds to the Arp1 subunit of dynactin
    • Holleran, E. A. et al. βIII spectrin binds to the Arp1 subunit of dynactin. J. Biol. Chem. 276, 36598-36605 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 36598-36605
    • Holleran, E.A.1
  • 7
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • DOI 10.1091/mbc.E05-03-0189
    • Johansson, M., Lehto, M., Tanhuanpaa, K., Cover, T. L. & Olkkonen, V. M. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol. Biol. Cell 16, 5480-5492 (2005). (Pubitemid 41752200)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpaa, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 9
    • 0034086882 scopus 로고    scopus 로고
    • Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport
    • Tsai, M. Y., Morfini, G., Szebenyi, G. & Brady, S. T. Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport. Mol. Biol. Cell 11, 2161-2173 (2000). (Pubitemid 30408071)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.6 , pp. 2161-2173
    • Tsai, M.-Y.1    Morfini, G.2    Szebenyi, G.3    Brady, S.T.4
  • 10
    • 37749000849 scopus 로고    scopus 로고
    • Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: A molecular model of kinesin-cargo release
    • Guillaud, L., Wong, R. & Hirokawa, N. Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release. Nat. Cell Biol. 10, 19-29 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 19-29
    • Guillaud, L.1    Wong, R.2    Hirokawa, N.3
  • 11
    • 33749510646 scopus 로고    scopus 로고
    • Regulatory dissociation of Tctex-1 light chain from dynein complex is essential for the apical delivery of rhodopsin
    • DOI 10.1111/j.1600-0854.2006.00482.x
    • Yeh, T. Y., Peretti, D., Chuang, J. Z., Rodriguez-Boulan, E. & Sung, C. H. Regulatory dissociation of Tctex-1 light chain from dynein complex is essential for the apical delivery of rhodopsin. Traffic 7, 1495-1502 (2006). (Pubitemid 44524522)
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1495-1502
    • Yeh, T.-Y.1    Peretti, D.2    Chuang, J.-Z.3    Rodriguez-Boulan, E.4    Sung, C.-H.5
  • 13
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • DOI 10.1083/jcb.200312034
    • Seaman, M. N. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111-122 (2004). (Pubitemid 38649181)
    • (2004) Journal of Cell Biology , vol.165 , Issue.1 , pp. 111-122
    • Seaman, M.N.J.1
  • 15
    • 71749090787 scopus 로고    scopus 로고
    • The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport
    • Hong, Z. et al. The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport. Cell Res. 19, 1334-1349 (2009).
    • (2009) Cell Res. , vol.19 , pp. 1334-1349
    • Hong, Z.1
  • 16
    • 56149112942 scopus 로고    scopus 로고
    • Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7
    • Rojas, R. et al. Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7. J. Cell Biol. 183, 513-526 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 513-526
    • Rojas, R.1
  • 17
  • 18
    • 67650218762 scopus 로고    scopus 로고
    • The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network
    • Wassmer, T. et al. The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network. Dev. Cell 17, 110-122 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 110-122
    • Wassmer, T.1
  • 19
    • 45849124923 scopus 로고    scopus 로고
    • Endosomal sorting and signalling: An emerging role for sorting nexins
    • DOI 10.1038/nrm2427, PII NRM2427
    • Cullen, P. J. Endosomal sorting and signalling: an emerging role for sorting nexins. Nat. Rev. Mol. Cell Biol. 9, 574-582 (2008). (Pubitemid 351881840)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.7 , pp. 574-582
    • Cullen, P.J.1
  • 21
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • DOI 10.1038/nature04397
    • Behnia, R. & Munro, S. Organelle identity and the signposts for membrane traffic. Nature 438, 597-604 (2005). (Pubitemid 41740563)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 22
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • DOI 10.1038/nature05185, PII NATURE05185
    • Di Paolo, G. & De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651-657 (2006). (Pubitemid 44564702)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 23
    • 77952396703 scopus 로고    scopus 로고
    • Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling
    • Szentpetery, Z., Varnai, P. & Balla, T. Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling. Proc. Natl Acad. Sci. USA 107, 8225-8230 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 8225-8230
    • Szentpetery, Z.1    Varnai, P.2    Balla, T.3
  • 25
    • 34347382638 scopus 로고    scopus 로고
    • PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal
    • DOI 10.1091/mbc.E06-10-0897
    • Wang, J. et al. PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal. Mol. Biol. Cell 18, 2646-2655 (2007). (Pubitemid 47025729)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.7 , pp. 2646-2655
    • Wang, J.1    Sun, H.-Q.2    Macia, E.3    Kirchhausen, T.4    Watson, H.5    Bonifacino, J.S.6    Yin, H.L.7
  • 26
    • 0037073673 scopus 로고    scopus 로고
    • The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation
    • DOI 10.1074/jbc.M206986200
    • Cozier, G. E. et al. The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation. J. Biol. Chem. 277, 48730-48736 (2002). (Pubitemid 35470838)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48730-48736
    • Cozier, G.E.1    Carlton, J.2    McGregor, A.H.3    Gleeson, P.A.4    Teasdale, R.D.5    Mellor, H.6    Cullen, P.J.7
  • 27
    • 0036701574 scopus 로고    scopus 로고
    • Phosphoinositides and the Golgi complex
    • DOI 10.1016/S0955-0674(02)00357-5
    • De Matteis, M., Godi, A. & Corda, D. Phosphoinositides and the Golgi complex. Curr. Opin. Cell Biol. 14, 434-447 (2002). (Pubitemid 35279103)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.4 , pp. 434-447
    • De Matteis, M.A.1    Godi, A.2    Corda, D.3
  • 28
    • 14844302797 scopus 로고    scopus 로고
    • A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: Studies with the PH domains of the oxysterol binding protein and FAPP1
    • DOI 10.1091/mbc.E04-07-0578
    • Balla, A., Tuymetova, G., Tsiomenko, A., Varnai, P. & Balla, T. A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III α: studies with the PH domains of the oxysterol binding protein and FAPP1. Mol. Biol. Cell 16, 1282-1295 (2005). (Pubitemid 40349564)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.3 , pp. 1282-1295
    • Balla, A.1    Tuymetova, G.2    Tsiomenko, A.3    Varnai, P.4    Balla, T.5
  • 29
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both Ptdlns 4-kinase-dependent and -independent components
    • DOI 10.1016/S0960-9822(02)00779-0, PII S0960982202007790
    • Levine, T. P. & Munro, S. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and-independent components. Curr. Biol. 12, 695-704 (2002). (Pubitemid 34455422)
    • (2002) Current Biology , vol.12 , Issue.9 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 30
    • 0037205494 scopus 로고    scopus 로고
    • Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments
    • DOI 10.1074/jbc.M111807200
    • Balla, A., Tuymetova, G., Barshishat, M., Geiszt, M. & Balla, T. Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments. J. Biol. Chem. 277, 20041-20050 (2002). (Pubitemid 34967528)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 20041-20050
    • Balla, A.1    Tuymetova, G.2    Barshishat, M.3    Geiszt, M.4    Balla, T.5
  • 31
    • 0029966103 scopus 로고    scopus 로고
    • Chromaffin granule-associated phosphatidylinositol 4-kinase activity is required for stimulated secretion
    • Wiedemann, C., Schafer, T. & Burger, M. M. Chromaffin granule-associated phosphatidylinositol 4-kinase activity is required for stimulated secretion. EMBO J. 15, 2094-2101 (1996). (Pubitemid 26141126)
    • (1996) EMBO Journal , vol.15 , Issue.9 , pp. 2094-2101
    • Wiedemann, C.1    Schafer, T.2    Burger, M.M.3
  • 32
    • 68749107213 scopus 로고    scopus 로고
    • Immunocytochemical techniques reveal multiple, distinct cellular pools of PtdIns4P and PtdIns(4,5)P(2)
    • Hammond, G. R., Schiavo, G. & Irvine, R. F. Immunocytochemical techniques reveal multiple, distinct cellular pools of PtdIns4P and PtdIns(4, 5)P(2). Biochem. J. 422, 23-35 (2009).
    • (2009) Biochem. J. , vol.422 , pp. 23-35
    • Hammond, G.R.1    Schiavo, G.2    Irvine, R.F.3
  • 33
    • 0029876888 scopus 로고    scopus 로고
    • Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases
    • DOI 10.1021/bi9517493
    • Downing, G. J., Kim, S., Nakanishi, S., Catt, K. J. & Balla, T. Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases. Biochemistry 35, 3587-3594 (1996). (Pubitemid 26092578)
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3587-3594
    • Downing, G.J.1    Kim, S.2    Nakanishi, S.3    Catt, K.J.4    Balla, T.5
  • 34
    • 0032570702 scopus 로고    scopus 로고
    • Differential regulation of muscarinic acetylcholine receptor-sensitive polyphosphoinositide pools and consequences for signaling in human neuroblastoma cells
    • DOI 10.1074/jbc.273.9.5037
    • Willars, G. B., Nahorski, S. R. & Challiss, R. A. Differential regulation of muscarinic acetylcholine receptor-sensitive polyphosphoinositide pools and consequences for signaling in human neuroblastoma cells. J. Biol. Chem. 273, 5037-5046 (1998). (Pubitemid 28108661)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.9 , pp. 5037-5046
    • Willars, G.B.1    Nahorski, S.R.2    Challiss, R.A.J.3
  • 35
    • 84864848873 scopus 로고    scopus 로고
    • 2 are essential but independent lipid determinants of membrane identity
    • 2 are essential but independent lipid determinants of membrane identity. Science 337, 727-730 (2012).
    • (2012) Science , vol.337 , pp. 727-730
    • Hammond, G.R.1
  • 36
    • 84864004215 scopus 로고    scopus 로고
    • Golgin160 recruits the dynein motor to position the Golgi apparatus
    • Yadav, S., Puthenveedu, M. A. & Linstedt, A. D. Golgin160 recruits the dynein motor to position the Golgi apparatus. Dev. Cell 23, 153-165 (2012).
    • (2012) Dev. Cell , vol.23 , pp. 153-165
    • Yadav, S.1    Puthenveedu, M.A.2    Linstedt, A.D.3
  • 38
    • 69949182309 scopus 로고    scopus 로고
    • The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4, 5-bisphosphate (PtdIns(45)P2)
    • Koharudin, L. M., Furey, W., Liu, H., Liu, Y. J. & Gronenborn, A. M. The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4, 5-bisphosphate (PtdIns(4, 5)P2). J. Biol. Chem. 284, 23697-23707 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 23697-23707
    • Koharudin, L.M.1    Furey, W.2    Liu, H.3    Liu, Y.J.4    Gronenborn, A.M.5
  • 41
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha, N. et al. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. J. Cell Biol. 185, 1209-1225 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 1209-1225
    • Rocha, N.1
  • 42
    • 79957914861 scopus 로고    scopus 로고
    • SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
    • Temkin, P. et al. SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nat. Cell Biol. 13, 715-721 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 715-721
    • Temkin, P.1
  • 43
    • 76149142505 scopus 로고    scopus 로고
    • PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking
    • Wood, C. S. et al. PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking. J. Cell Biol. 187, 967-975 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 967-975
    • Wood, C.S.1
  • 44
    • 84863011642 scopus 로고    scopus 로고
    • Myosin i links PIP3 signaling to remodeling of the actin cytoskeleton in chemotaxis
    • Chen, C. L., Wang, Y., Sesaki, H. & Iijima, M. Myosin I links PIP3 signaling to remodeling of the actin cytoskeleton in chemotaxis. Science Signal. 5, ra10 (2012).
    • (2012) Science Signal. , vol.5
    • Chen, C.L.1    Wang, Y.2    Sesaki, H.3    Iijima, M.4
  • 45
    • 0034622674 scopus 로고    scopus 로고
    • GAP1IP4BP contains a novel group i pleckstrin homology domain that directs constitutive plasma membrane association
    • Cozier, G. E. et al. GAP1IP4BP contains a novel group I pleckstrin homology domain that directs constitutive plasma membrane association. J. Biol. Chem. 275, 28261-28268 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 28261-28268
    • Cozier, G.E.1
  • 46
    • 79955880405 scopus 로고    scopus 로고
    • Sequential interactions with Sec23 control the direction of vesicle traffic
    • Lord, C. et al. Sequential interactions with Sec23 control the direction of vesicle traffic. Nature 473, 181-186 (2011).
    • (2011) Nature , vol.473 , pp. 181-186
    • Lord, C.1
  • 48
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • Stefan, C. J. et al. Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites. Cell 144, 389-401 (2011).
    • (2011) Cell , vol.144 , pp. 389-401
    • Stefan, C.J.1
  • 49
    • 80755129133 scopus 로고    scopus 로고
    • A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes
    • Kim, Y. J., Guzman-Hernandez, M.L. & Balla, T. A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes. Dev. Cell 21, 813-824 (2011).
    • (2011) Dev. Cell , vol.21 , pp. 813-824
    • Kim, Y.J.1    Guzman-Hernandez, M.L.2    Balla, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.