메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYTOCHALASIN D; F ACTIN; MYOSIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; DROSOPHILA PROTEIN; WASP PROTEIN, DROSOPHILA; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 84949502652     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10098     Document Type: Article
Times cited : (71)

References (51)
  • 1
    • 84859615146 scopus 로고    scopus 로고
    • Regulated exocytosis: Novel insights from intravital microscopy
    • Masedunskas A., Porat-Shliom N., & Weigert R. Regulated exocytosis: novel insights from intravital microscopy. Traffic 13, 627-634 (2012
    • (2012) Traffic , vol.13 , pp. 627-634
    • Masedunskas, A.1    Porat-Shliom, N.2    Weigert, R.3
  • 2
    • 84861770398 scopus 로고    scopus 로고
    • Actin coats and rings promote regulated exocytosis
    • Nightingale T. D., Cutler D. F., & Cramer L. P. Actin coats and rings promote regulated exocytosis. Trends Cell Biol. 22, 329-337 (2012
    • (2012) Trends Cell Biol , vol.22 , pp. 329-337
    • Nightingale, T.D.1    Cutler, D.F.2    Cramer, L.P.3
  • 3
    • 84878603047 scopus 로고    scopus 로고
    • Multiple roles for the actin cytoskeleton during regulated exocytosis
    • Porat-Shliom N., Milberg O., Masedunskas A., & Weigert R. Multiple roles for the actin cytoskeleton during regulated exocytosis. Cell Mol. Life Sci. 70, 2099-2121 (2013
    • (2013) Cell Mol. Life Sci , vol.70 , pp. 2099-2121
    • Porat-Shliom, N.1    Milberg, O.2    Masedunskas, A.3    Weigert, R.4
  • 4
    • 80053325995 scopus 로고    scopus 로고
    • Remodelling of cortical actin where lytic granules dock at natural killer cell immune synapses revealed by super-resolution microscopy
    • Brown A. C., et al. Remodelling of cortical actin where lytic granules dock at natural killer cell immune synapses revealed by super-resolution microscopy. PLoS Biol. 9, e1001152 (2011
    • (2011) Plos Biol , vol.9 , pp. e1001152
    • Brown, A.C.1
  • 5
    • 23744437503 scopus 로고    scopus 로고
    • Real-time dynamics of the F-actin cytoskeleton during secretion from chromaffin cells
    • Giner D., et al. Real-time dynamics of the F-actin cytoskeleton during secretion from chromaffin cells. J. Cell Sci. 118, 2871-2880 (2005
    • (2005) J. Cell Sci , vol.118 , pp. 2871-2880
    • Giner, D.1
  • 6
    • 38549147387 scopus 로고    scopus 로고
    • Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells
    • Trifaro J. M., Gasman S., & Gutierrez L. M. Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells. Acta Physiol. (Oxf) 192, 165-172 (2008
    • (2008) Acta Physiol. (Oxf , vol.192 , pp. 165-172
    • Trifaro, J.M.1    Gasman, S.2    Gutierrez, L.M.3
  • 7
    • 0041989574 scopus 로고    scopus 로고
    • Cdc42-dependent actin polymerization during compensatory endocytosis in xenopus eggs
    • Sokac A. M., Co C., Taunton J., & Bement W. Cdc42-dependent actin polymerization during compensatory endocytosis in Xenopus eggs. Nat. Cell Biol. 5, 727-732 (2003
    • (2003) Nat. Cell Biol , vol.5 , pp. 727-732
    • Sokac, A.M.1    Co, C.2    Taunton, J.3    Bement, W.4
  • 8
    • 33750487863 scopus 로고    scopus 로고
    • Myosin-1c couples assembling actin to membranes to drive compensatory endocytosis
    • Sokac A. M., Schietroma C., Gundersen C. B., & Bement W. M. Myosin-1c couples assembling actin to membranes to drive compensatory endocytosis. Dev. Cell 11, 629-640 (2006
    • (2006) Dev. Cell , vol.11 , pp. 629-640
    • Sokac, A.M.1    Schietroma, C.2    Gundersen, C.B.3    Bement, W.M.4
  • 9
    • 33947258860 scopus 로고    scopus 로고
    • Control of local actin assembly by membrane fusion-dependent compartment mixing
    • Yu H. Y., & Bement W. M. Control of local actin assembly by membrane fusion-dependent compartment mixing. Nat. Cell Biol. 9, 149-159 (2007
    • (2007) Nat. Cell Biol , vol.9 , pp. 149-159
    • Yu, H.Y.1    Bement, W.M.2
  • 10
    • 34948864330 scopus 로고    scopus 로고
    • Multiple myosins are required to coordinate actin assembly with coat compression during compensatory endocytosis
    • Yu H. Y., & Bement W. M. Multiple myosins are required to coordinate actin assembly with coat compression during compensatory endocytosis. Mol. Biol. Cell 18, 4096-4105 (2007
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4096-4105
    • Yu, H.Y.1    Bement, W.M.2
  • 11
    • 27844523175 scopus 로고    scopus 로고
    • Actin and non-muscle myosin II facilitate apical exocytosis of tear proteins in rabbit lacrimal acinar epithelial cells
    • Jerdeva G. V., et al. Actin and non-muscle myosin II facilitate apical exocytosis of tear proteins in rabbit lacrimal acinar epithelial cells. J. Cell Sci. 118, 4797-4812 (2005
    • (2005) J. Cell Sci , vol.118 , pp. 4797-4812
    • Jerdeva, G.V.1
  • 12
    • 84925422795 scopus 로고    scopus 로고
    • Actin depolymerisation and crosslinking join forces with myosin II to contract actin coats on fused secretory vesicles
    • Miklavc P., et al. Actin depolymerisation and crosslinking join forces with myosin II to contract actin coats on fused secretory vesicles. J. Cell Sci. 128, 1193-1203 (2015
    • (2015) J. Cell Sci , vol.128 , pp. 1193-1203
    • Miklavc, P.1
  • 13
    • 84864976385 scopus 로고    scopus 로고
    • Actin coating and compression of fused secretory vesicles are essential for surfactant secretion-A role for rho, formins and myosin II
    • Miklavc P., et al. Actin coating and compression of fused secretory vesicles are essential for surfactant secretion-a role for Rho, formins and myosin II. J. Cell Sci. 125, 2765-2774 (2012
    • (2012) J. Cell Sci , vol.125 , pp. 2765-2774
    • Miklavc, P.1
  • 14
    • 80052614265 scopus 로고    scopus 로고
    • Actomyosin II contractility expels von willebrand factor from weibel-palade bodies during exocytosis
    • Nightingale T. D., et al. Actomyosin II contractility expels von Willebrand factor from Weibel-Palade bodies during exocytosis. J. Cell Biol. 194, 613-629 (2011
    • (2011) J. Cell Biol , vol.194 , pp. 613-629
    • Nightingale, T.D.1
  • 15
    • 34548508978 scopus 로고    scopus 로고
    • Dynamic regulation of the large exocytotic fusion pore in pancreatic acinar cells
    • Larina O., et al. Dynamic regulation of the large exocytotic fusion pore in pancreatic acinar cells. Mol. Biol. Cell 18, 3502-3511 (2007
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3502-3511
    • Larina, O.1
  • 16
    • 80052017958 scopus 로고    scopus 로고
    • Role for the actomyosin complex in regulated exocytosis revealed by intravital microscopy
    • Masedunskas A., et al. Role for the actomyosin complex in regulated exocytosis revealed by intravital microscopy. Proc. Natl Acad. Sci. USA 108, 13552-13557 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13552-13557
    • Masedunskas, A.1
  • 17
    • 33646864565 scopus 로고    scopus 로고
    • Staying in shape with formins
    • Faix J., & Grosse R. Staying in shape with formins. Dev. Cell 10, 693-706 (2006
    • (2006) Dev. Cell , vol.10 , pp. 693-706
    • Faix, J.1    Grosse, R.2
  • 18
    • 0032479425 scopus 로고    scopus 로고
    • Identification of a potential effector pathway for the trimeric go protein associated with secretory granules go stimulates a granule-bound phosphatidylinositol 4-kinase by activating rhoa in chromaffin cells
    • Gasman S., Chasserot-Golaz S., Hubert P., Aunis D., & Bader M. F. Identification of a potential effector pathway for the trimeric Go protein associated with secretory granules. Go stimulates a granule-bound phosphatidylinositol 4-kinase by activating RhoA in chromaffin cells. J. Biol. Chem. 273, 16913-16920 (1998
    • (1998) J. Biol. Chem , vol.273 , pp. 16913-16920
    • Gasman, S.1    Chasserot-Golaz, S.2    Hubert, P.3    Aunis, D.4    Bader, M.F.5
  • 19
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode B. L., & Eck M. J. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76, 593-627 (2007
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 20
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: An actin nucleator comes of age
    • Goley E. D., & Welch M. D. The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 7, 713-726 (2006
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 21
    • 70849098888 scopus 로고    scopus 로고
    • Actin a central player in cell shape and movement
    • Pollard T. D., & Cooper J. A. Actin, a central player in cell shape and movement. Science 326, 1208-1212 (2009
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 22
    • 79951556468 scopus 로고    scopus 로고
    • New mechanisms and functions of actin nucleation
    • Firat-Karalar E. N., & Welch M. D. New mechanisms and functions of actin nucleation. Curr. Opin. Cell Biol. 23, 4-13 (2011
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 4-13
    • Firat-Karalar, E.N.1    Welch, M.D.2
  • 23
  • 24
    • 84871519238 scopus 로고    scopus 로고
    • New insights into the regulation and cellular functions of the ARP2/3 complex
    • Rotty J. D., Wu C., & Bear J. E. New insights into the regulation and cellular functions of the ARP2/3 complex. Nat. Rev. Mol. Cell Biol. 14, 7-12 (2013
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 7-12
    • Rotty, J.D.1    Wu, C.2    Bear, J.E.3
  • 25
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by arp2/3 complex and wasp/scar proteins
    • Blanchoin L., et al. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404, 1007-1011 (2000
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1
  • 26
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins R. D., Heuser J. A., & Pollard T. D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl Acad. Sci. USA 95, 6181-6186 (1998
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 27
    • 84883681341 scopus 로고    scopus 로고
    • Actin dynamics regulated by the balance of neuronal Wiskott- Aldrich syndrome protein (N-WASP) and cofilin activities determines the biphasic response of glucose-induced insulin secretion
    • Uenishi E., et al. Actin dynamics regulated by the balance of neuronal Wiskott- Aldrich syndrome protein (N-WASP) and cofilin activities determines the biphasic response of glucose-induced insulin secretion. J. Biol. Chem. 288, 25851-25864 (2013
    • (2013) J. Biol. Chem , vol.288 , pp. 25851-25864
    • Uenishi, E.1
  • 28
    • 22844442923 scopus 로고    scopus 로고
    • Parotid secretory granules: Crossroads of secretory pathways and protein storage
    • Gorr S. U., Venkatesh S. G., & Darling D. S. Parotid secretory granules: crossroads of secretory pathways and protein storage. J. Dent. Res. 84, 500-509 (2005
    • (2005) J. Dent. Res , vol.84 , pp. 500-509
    • Gorr, S.U.1    Venkatesh, S.G.2    Darling, D.S.3
  • 29
    • 84864292544 scopus 로고    scopus 로고
    • Type II phosphatidylinositol 4-kinase regulates trafficking of secretory granule proteins in Drosophila
    • Burgess J., et al. Type II phosphatidylinositol 4-kinase regulates trafficking of secretory granule proteins in Drosophila. Development 139, 3040-3050 (2012
    • (2012) Development , vol.139 , pp. 3040-3050
    • Burgess, J.1
  • 30
    • 79959250824 scopus 로고    scopus 로고
    • AP-1 and clathrin are essential for secretory granule biogenesis in Drosophila
    • Burgess J., et al. AP-1 and clathrin are essential for secretory granule biogenesis in Drosophila. Mol. Biol. Cell 22, 2094-2105 (2011
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2094-2105
    • Burgess, J.1
  • 32
    • 0035282129 scopus 로고    scopus 로고
    • Glue secretion in the Drosophila salivary gland: A model for steroid-regulated exocytosis
    • Biyasheva A., Do T. V., Lu Y., Vaskova M., & Andres A. J. Glue secretion in the Drosophila salivary gland: a model for steroid-regulated exocytosis. Dev. Biol. 231, 234-251 (2001
    • (2001) Dev. Biol , vol.231 , pp. 234-251
    • Biyasheva, A.1    Do, T.V.2    Lu, Y.3    Vaskova, M.4    Andres, A.J.5
  • 33
    • 0000012353 scopus 로고
    • The hormonal control of salivary gland secretion in Drosophila melanogaster: Studies in vitro
    • Boyd M., & Ashburner M. The hormonal control of salivary gland secretion in Drosophila melanogaster: studies in vitro. J. Insect Physiol. 23, 517-523 (1977
    • (1977) J. Insect Physiol , vol.23 , pp. 517-523
    • Boyd, M.1    Ashburner, M.2
  • 34
    • 78951491636 scopus 로고    scopus 로고
    • The Drosophila blood brain barrier is maintained by GPCR-dependent dynamic actin structures
    • Hatan M., Shinder V., Israeli D., Schnorrer F., & Volk T. The Drosophila blood brain barrier is maintained by GPCR-dependent dynamic actin structures. J. Cell Biol. 192, 307-319 (2011
    • (2011) J. Cell Biol , vol.192 , pp. 307-319
    • Hatan, M.1    Shinder, V.2    Israeli, D.3    Schnorrer, F.4    Volk, T.5
  • 35
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl J., et al. Lifeact: a versatile marker to visualize F-actin. Nat. Methods 5, 605-607 (2008
    • (2008) Nat. Methods , vol.5 , pp. 605-607
    • Riedl, J.1
  • 36
    • 77950590834 scopus 로고    scopus 로고
    • Vesicle adsorption and phospholipid bilayer formation on topographically and chemically nanostructured surfaces
    • Pfeiffer I., Petronis S., Koper I., Kasemo B., & Zach M. Vesicle adsorption and phospholipid bilayer formation on topographically and chemically nanostructured surfaces. J. Phys. Chem. B 114, 4623-4631 (2010
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4623-4631
    • Pfeiffer, I.1    Petronis, S.2    Koper, I.3    Kasemo, B.4    Zach, M.5
  • 38
    • 84901408334 scopus 로고    scopus 로고
    • PI 4 5)P2 regulates myoblast fusion through Arp2/3 regulator localization at the fusion site
    • Bothe I., Deng S., & Baylies M. PI (4,5)P2 regulates myoblast fusion through Arp2/3 regulator localization at the fusion site. Development 141, 2289-2301 (2014
    • (2014) Development , vol.141 , pp. 2289-2301
    • Bothe, I.1    Deng, S.2    Baylies, M.3
  • 39
    • 0034683671 scopus 로고    scopus 로고
    • Activation by cdc42 and pip(2) of wiskott- aldrich syndrome protein (wasp) stimulates actin nucleation by arp2/3 complex
    • Higgs H. N., & Pollard T. D. Activation by Cdc42 and PIP(2) of Wiskott- Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150, 1311-1320 (2000
    • (2000) J. Cell Biol , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 40
    • 67651124954 scopus 로고    scopus 로고
    • Tweek, an evolutionarily conserved protein, is required for synaptic vesicle recycling
    • Verstreken P., et al. Tweek, an evolutionarily conserved protein, is required for synaptic vesicle recycling. Neuron 63, 203-215 (2009
    • (2009) Neuron , vol.63 , pp. 203-215
    • Verstreken, P.1
  • 41
    • 34249027579 scopus 로고    scopus 로고
    • The carnegie protein trap library: A versatile tool for Drosophila developmental studies
    • Buszczak M., et al. The carnegie protein trap library: a versatile tool for Drosophila developmental studies. Genetics 175, 1505-1531 (2007
    • (2007) Genetics , vol.175 , pp. 1505-1531
    • Buszczak, M.1
  • 42
    • 85027917466 scopus 로고    scopus 로고
    • An Arf-GEF regulates antagonism between endocytosis and the cytoskeleton for Drosophila blastoderm development
    • Lee D. M., & Harris T. J. An Arf-GEF regulates antagonism between endocytosis and the cytoskeleton for Drosophila blastoderm development. Curr. Biol. 23, 2110-2120 (2013
    • (2013) Curr. Biol , vol.23 , pp. 2110-2120
    • Lee, D.M.1    Harris, T.J.2
  • 44
    • 84903179661 scopus 로고    scopus 로고
    • Intestinal MUC2 mucin supramolecular topology by packing and release resting on D3 domain assembly
    • Nilsson H. E., et al. Intestinal MUC2 mucin supramolecular topology by packing and release resting on D3 domain assembly. J. Mol. Biol. 426, 2567-2579 (2014
    • (2014) J. Mol. Biol , vol.426 , pp. 2567-2579
    • Nilsson, H.E.1
  • 45
    • 84858847376 scopus 로고    scopus 로고
    • New insights into the role of the cortical cytoskeleton in exocytosis from neuroendocrine cells
    • Gutierrez L. M. New insights into the role of the cortical cytoskeleton in exocytosis from neuroendocrine cells. Int. Rev. Cell Mol. Biol. 295, 109-137 (2012
    • (2012) Int. Rev. Cell Mol. Biol , vol.295 , pp. 109-137
    • Gutierrez, L.M.1
  • 46
    • 84863618181 scopus 로고    scopus 로고
    • Real-time measurement of F-actin remodelling during exocytosis using Lifeact-EGFP transgenic animals
    • Jang Y., Soekmadji C., Mitchell J. M., Thomas W. G., & Thorn P. Real-time measurement of F-actin remodelling during exocytosis using Lifeact-EGFP transgenic animals. PLoS ONE 7, e39815 (2012
    • (2012) Plos One , vol.7 , pp. e39815
    • Jang, Y.1    Soekmadji, C.2    Mitchell, J.M.3    Thomas, W.G.4    Thorn, P.5
  • 47
    • 84859613830 scopus 로고    scopus 로고
    • Calcium and ph-dependent packing and release of the gel-forming muc2 mucin
    • Ambort D., et al. Calcium and pH-dependent packing and release of the gel-forming MUC2 mucin. Proc. Natl Acad. Sci. USA 109, 5645-5650 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 5645-5650
    • Ambort, D.1
  • 48
    • 84906707282 scopus 로고    scopus 로고
    • Microbial-induced meprin beta cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus
    • Schutte A., et al. Microbial-induced meprin beta cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus. Proc. Natl Acad. Sci. USA 111, 12396-12401 (2014
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 12396-12401
    • Schutte, A.1
  • 49
    • 67650081142 scopus 로고    scopus 로고
    • The arp2/3 complex and wasp are required for apical trafficking of delta into microvilli during cell fate specification of sensory organ precursors
    • Rajan A., Tien A. C., Haueter C. M., Schulze K. L., & Bellen H. J. The Arp2/3 complex and WASp are required for apical trafficking of Delta into microvilli during cell fate specification of sensory organ precursors. Nat Cell Biol. 11, 815-824 (2009
    • (2009) Nat Cell Biol , vol.11 , pp. 815-824
    • Rajan, A.1    Tien, A.C.2    Haueter, C.M.3    Schulze, K.L.4    Bellen, H.J.5
  • 50
    • 34447530305 scopus 로고    scopus 로고
    • A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila
    • Dietzl G., et al. A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila. Nature 448, 151-156 (2007
    • (2007) Nature , vol.448 , pp. 151-156
    • Dietzl, G.1
  • 51
    • 0037197947 scopus 로고    scopus 로고
    • Arp2/3-dependent pseudocleavage furrow assembly in syncytial drosophila embryos
    • Stevenson V., Hudson A., Cooley L., & Theurkauf W. E. Arp2/3-dependent pseudocleavage furrow assembly in syncytial Drosophila embryos. Curr. Biol. 12, 705-711 (2002
    • (2002) Curr. Biol , vol.12 , pp. 705-711
    • Stevenson, V.1    Hudson, A.2    Cooley, L.3    Theurkauf, W.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.