View Item 

Show simple item record

Facilitation of Ca 2+ -dependent exocytosis by Rac1-GTPase in bovine chromaffin cells

dc.contributor.authorLi, Quanwenen_US
dc.contributor.authorHo, Chi S.en_US
dc.contributor.authorMarinescu, Vladen_US
dc.contributor.authorBhatti, Humaaen_US
dc.contributor.authorBokoch, Gary M.en_US
dc.contributor.authorErnst, Stephen A.en_US
dc.contributor.authorHolz, Ronald W.en_US
dc.contributor.authorStuenkel, Edward L.en_US
dc.date.accessioned2010-04-01T15:37:25Z
dc.date.available2010-04-01T15:37:25Z
dc.date.issued2003-07en_US
dc.identifier.citationLi, Quanwen; Ho, Chi S.; Marinescu, Vlad; Bhatti, Humaa; Bokoch, Gary M.; Ernst, Stephen A.; Holz, Ronald W.; Stuenkel, Edward L. (2003). "Facilitation of Ca 2+ -dependent exocytosis by Rac1-GTPase in bovine chromaffin cells." The Journal of Physiology 550(2): 431-445. <http://hdl.handle.net/2027.42/66111>en_US
dc.identifier.issn0022-3751en_US
dc.identifier.issn1469-7793en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/66111
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=12754309&dopt=citationen_US
dc.format.extent656396 bytes
dc.format.extent3110 bytes
dc.format.mimetypeapplication/octet-stream
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rightsThe Physiological Society 2003en_US
dc.titleFacilitation of Ca 2+ -dependent exocytosis by Rac1-GTPase in bovine chromaffin cellsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPhysiologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationum* Department of Physiology, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationum† Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationum§ Department of Pharmacology, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationother† Department of Immunology and Cell Biology, The Scripps Research Institute, La Jolla, CA, USAen_US
dc.identifier.pmid12754309en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/66111/1/jphysiol.2003.039073.pdf
dc.identifier.doi10.1113/jphysiol.2003.039073en_US
dc.identifier.sourceThe Journal of Physiologyen_US
dc.identifier.citedreferenceBenard V, Bohl BP & Bokoch GM ( 1999 ). Characterization of Rac and Cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J Biol Chem 274, 13198 – 13204.en_US
dc.identifier.citedreferenceBernstein BW, & Bamburg JR ( 1985 ). Reorganization of actin in depolarized synaptosomes. J Neurosci 5, 2565 – 2569.en_US
dc.identifier.citedreferenceBoguski MS, & McCormick, F ( 1993 ). Proteins regulating Ras and its relatives. Nature 366, 643 – 654.en_US
dc.identifier.citedreferenceBrown AM, O'Sullivan AJ & Gomperts BD ( 1998 ). Induction of exocytosis from permeabilized mast cells by the guanosine triphosphatases Rac and Cdc42. Mol Biol Cell 9, 1053 – 1063.en_US
dc.identifier.citedreferenceBuchanan FG, Elliot CM, Gibbs M & Exton JH ( 2000 ). Translocation of the Rac1 guanine nucleotide exchange factor Tiam1 induced by platelet-derived growth factor and lysophosphatidic acid. J Biol Chem 275, 9742 – 9748.en_US
dc.identifier.citedreferenceCarpenter CL, Tolias KF, Van Vugt A & Hartwig J ( 1999 ). Lipid kinases are novel effectors of the GTPase Rac1. Adv Enzyme Regul 39, 299 – 312.en_US
dc.identifier.citedreferenceChasserot-Golaz S, Hubert P, Thierse D, Dirrig S, Vlahos CJ, Aunis D & Bader MF ( 1998 ). Possible involvement of phosphatidylinositol 3-kinase in regulated exocytosis: studies in chromaffin cells with inhibitor LY294002. J Neurochem 70, 2347 – 2356.en_US
dc.identifier.citedreferenceCheek TR, ( 1991 ). Calcium signalling and the triggering of secretion in adrenal chromaffin cells. Pharmacol Ther 52, 173 – 189.en_US
dc.identifier.citedreferenceCheek TR, & Burgoyne RD ( 1986 ). Nicotine-evoked disassembly of cortical actin filamanets in adrenal chromaffin cells. FEBS Lett 207, 110 – 114.en_US
dc.identifier.citedreferenceChowdhury HH, Kreft M & Zorec R ( 2002 ). Distinct effect of actin cytoskeleton disassembly on exo- and endocytic events in a membrane patch of rat melanotrophs. J Physiol 545, 879 – 886.en_US
dc.identifier.citedreferenceChowdhury HH, Popoff MR & Zorec R ( 1999 ). Actin cytoskeleton depolymerization with Clostridium spiroforme toxin enhances the secretory activity of rat melanotrophs. J Physiol 521, 389 – 395.en_US
dc.identifier.citedreferenceDoussau F, Gasman S, Humeau Y, Vitiello F, Popoff M, Boquet P, Bader M-F & Poulain B ( 2000 ). A Rho-related GTPase is involved in Ca 2+ -dependent neurotransmitter exocytosis. J Biol Chem 275, 7764 – 7720.en_US
dc.identifier.citedreferenceEberhard DA, Cooper CL, Low MG & Holz RW ( 1990 ). Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP. Biochem J 268, 15 – 25.en_US
dc.identifier.citedreferenceEberhard DA, & Holz RW ( 1991 ). Regulation of the formation of inositol phosphates by calcium, guanine nucleotides and ATP in digitonin-permeabilized bovine adrenal chromaffin cells. Biochem J 279, 447 – 453.en_US
dc.identifier.citedreferenceEngisch KL, Chernevskaya NI & Nowycky MC ( 1997 ). Short-term changes in the Ca 2+ -exocytosis relationship during repetitive pulse protocols in bovine adrenal chromaffin cells. J Neurosci 17, 9010 – 9025.en_US
dc.identifier.citedreferenceFleming IN, Elliott CM, Buchanan FG, Downes CP & Exton JH ( 1999 ). Ca 2+ /calmodulin-dependent protein kinase II regulates Tiam1 by reversible protein phosphorylation. J Biol Chem 274, 12753 – 12758.en_US
dc.identifier.citedreferenceFrantz C, Coppola T & Regazzi R ( 2002 ). Involvement of Rho GTPases and their effectors in the secretory process of PC12 cells. Exp Cell Res 273, 119 – 126.en_US
dc.identifier.citedreferenceGasman S, Chasserot-Golaz S, Popoff MR, Aunis D & Bader M-F ( 1999 ). Involvement of Rho GTPases in calcium-regulated exocytosis from adrenal chromaffin cells. J Cell Sci 112, 4763 – 4771.en_US
dc.identifier.citedreferenceGil A, Rueda J, Viniegra S & Gutierrez LM ( 2000 ). The F-actin cytoskeleton modulates slow secretory components rather than readily releasable vesicle pools in bovine chromaffin cells. Neuroscience 98, 605 – 614.en_US
dc.identifier.citedreferenceGuillemot JP, Montcourrier P, Vivier E, Davoust J & Chavrier P ( 1997 ). Selective control of membrane ruffling and actin plaque assembly by the Rho GTPases Rac1 and Cdc42 in Fc e RI-activated rat basophilic leukemia (RBL-2H3) cells. J Cell Sci 110, 2215 – 2225.en_US
dc.identifier.citedreferenceHall A, ( 1994 ). Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu Rev Cell Biol 10, 31 – 54.en_US
dc.identifier.citedreferenceHall A, ( 1998 ). Rho GTPases and the actin cytoskeleton. Science 279, 509 – 514.en_US
dc.identifier.citedreferenceHammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA & Morris AJ ( 1997 ). Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4, 5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem 272, 3860 – 3868.en_US
dc.identifier.citedreferenceHay JC, Fisette PL, Jenkins GH, Fukami K, Takenawa T, Anderson RA & Martin TF ( 1995 ). ATP-dependent inositide phosphorylation required for Ca 2+ -activated secretion. Nature 374, 173 – 177.en_US
dc.identifier.citedreferenceHay JC, & Martin TF ( 1993 ). Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca 2+ -activated secretion. Nature 366, 572 – 575.en_US
dc.identifier.citedreferenceHayashi K, Ohshima T & Mikoshiba K ( 2002 ). Pak1 is involved in dendrite initiation as a downstream effector of Rac1 in cortical neurons. Mol Cell Neurosci 20, 579 – 594.en_US
dc.identifier.citedreferenceHolz RW, Brondyk WH, Senter RA, Kuizon L & Macara IG ( 1994 ). Evidence for the involvement of Rab3A in Ca 2+ -dependent exocytosis from adrenal chromaffin cells. J Biol Chem 269, 10229 – 10234.en_US
dc.identifier.citedreferenceHolz RW, Hlubek MD, Sorensen SD, Fisher SK, Balla T, Ozaki S, Prestwich GD, Stuenkel EL & Bittner MA ( 2000 ). A pleckstrin homology domain specific for phosphatidylinositol 4, 5-bisphosphate (PtdIns-4, 5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4, 5-P2 as being important in exocytosis. J Biol Chem 275, 17878 – 17885.en_US
dc.identifier.citedreferenceHong-Geller E, & Cerione RA ( 2000 ). Cdc42 and Rac stimulate exocytosis of secretory granules by activating the IP3/calcium pathway in RBL-2H3 mast cells. J Cell Biol 148, 481 – 493.en_US
dc.identifier.citedreferenceHumeau Y, Popoff MR, Kojima H, Doussau F & Poulain B ( 2002 ). Rac GTPase plays an essential role in exocytosis by controlling the fusion competence of release sites. J Neurosci 22, 7968 – 7981.en_US
dc.identifier.citedreferenceHumeau Y, Vitale N, Chasserot-Golaz S, Dupont JL, Du G, Frohman MA, Bader MF & Poulain B ( 2001 ). A role for phospholipase D1 in neurotransmitter release. Proc Natl Acad Sci U S A 98, 15300 – 15305.en_US
dc.identifier.citedreferenceIllenberger D, Schwald F & Gierschik P ( 1997 ). Characterization and purification from bovine neutrophils of a soluble guanine-nucleotide-binding protein that mediates isozyme-specific stimulation of phospholipase C beta2. Eur J Biochem 246, 71 – 77.en_US
dc.identifier.citedreferenceIllenberger D, Schwald F, Pimmer D, Binder W, Maier G, Dietrich A & Gierschik P ( 1998 ). Stimulation of phospholipase C-beta2 by the Rho GTPases Cdc42Hs and Rac1. EMBO J 17, 6241 – 6249.en_US
dc.identifier.citedreferenceIllenberger D, Stephan I, Gierschik P & Schwald F ( 2000 ). Stimulation of phospholipase C-beta 2 by Rho GTPases. Methods Enzymol 325, 167 – 177.en_US
dc.identifier.citedreferenceJoneson T, McDonough M, Bar-Sagi D & Van Aelst L ( 1996 ). RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science 274, 1374 – 1376.en_US
dc.identifier.citedreferenceJungermann J, Lerch MM, Weidenbach H, Lutz MP, Kruger B & Adler G ( 1995 ). Disassembly of rat pancreatic acinar cell cytoskeleton during supramaximal secretagogue stimulation. Am J Physiol 268, G328 – 338.en_US
dc.identifier.citedreferenceKaibuchi K, Kuroda S & Amano M ( 1999 ). Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu Rev Biochem 68, 459 – 486.en_US
dc.identifier.citedreferenceKowluru A, Li G, Rabaglia ME, Segu VB, Hofmann F, Aktories K & Metz SA ( 1997 ). Evidence for differential roles of the Rho subfamily of GTP-binding proteins in glucose- and calcium-induced insulin secretion from pancreatic Β cells. Biochem Pharmacol 54, 1097 – 1108.en_US
dc.identifier.citedreferenceLaemmli UK, ( 1970 ). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 – 685.en_US
dc.identifier.citedreferenceLamarche N, Tapon N, Stowers L, Burbelo PD, Aspenstrom P, Bridges T, Chant J & Hall A ( 1996 ). Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell 87, 519 – 529.en_US
dc.identifier.citedreferenceLang T, Wacker I, Wunderlich I, Rohrbach A, Giese G, Soldati T & Almers W ( 2000 ). Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells. Biophys J 78, 2863 – 2877.en_US
dc.identifier.citedreferenceLelkes PI, Friedman JE, Rosenheck K & Oplatka A ( 1986 ). Destabilization of actin filaments as a requirement for the secretion of catecholamines from permeabilized chromaffin cells. FEBS Lett 208, 357 – 363.en_US
dc.identifier.citedreferenceMackay DJ, & Hall A ( 1998 ). Rho GTPases. J Biol Chem 273, 20685 – 20688.en_US
dc.identifier.citedreferenceMuallem S, Kwiatkowska K, Xu X & Yin HL ( 1995 ). Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. J Cell Biol 128, 589 – 598.en_US
dc.identifier.citedreferenceNakata T, & Hirokawa N ( 1992 ). Organization of cortical cytoskeleton of cultured chromaffin cells and involvement in secretion as revealed by quick-freeze, deep-etching, and double-label immunoelectron microscopy. J Neurosci 12, 2186 – 2197.en_US
dc.identifier.citedreferenceNobes CD, & Hall A ( 1995 ). Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53 – 62.en_US
dc.identifier.citedreferenceNorman JC, Price LS, Ridley AJ, Hall A & Koffer A ( 1994 ). Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J Cell Biol 126, 1005 – 1015.en_US
dc.identifier.citedreferenceNorman JC, Price LS, Ridley AJ & Koffer A ( 1996 ). The small GTP-binding proteins Rac and Rho, regulate cytoskeletal organizaation and exocytosis in mast cells by parallel pathways. Mol Biol Cell 7, 1429 – 1442.en_US
dc.identifier.citedreferenceO'Sullivan AJ, Brown AM, Freeman HN & Gomperts BD ( 1996 ). Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a rac/rhoGDI complex. Mol Biol Cell 7, 397 – 408.en_US
dc.identifier.citedreferencePinxteren JA, O'Sullivan AJ, Larbi KY, Tatham PE & Gomperts BD ( 2000 ). Thirty years of stimulus-secretion coupling: from Ca 2+ to GTP in the regulation of exocytosis. Biochimie 82, 385 – 393.en_US
dc.identifier.citedreferencePlattner H, Artalejo AR & Neher E ( 1997 ). Ultrastructural organization of bovine chromaffin cell cortex-analysis by cryofixation and morphometry of aspects pertinent to exocytosis [published erratum appears in J Cell Biol (1998) 140, 973]. J Cell Biol 139, 1709 – 1717.en_US
dc.identifier.citedreferencePrepens U, Just I, Von Eichel-Streiber C & Aktories K ( 1996 ). Inhibition of Fc e RI-mediated activation of rat basophilic leukemia cells by Clostridium difficile toxin B (monoglucosyltransferase). J Biol Chem 271, 7324 – 7329.en_US
dc.identifier.citedreferencePrice LS, Norman JC, Ridley AC & Koffer A ( 1995 ). The small GTPases Rac and Rho as regulators of secretion in mast cells. Curr Biol 5, 68 – 73.en_US
dc.identifier.citedreferenceRen XD, & Schwartz MA ( 1998 ). Regulation of inositol lipid kinases by Rho and Rac. Curr Opin Genet Dev 8, 63 – 67.en_US
dc.identifier.citedreferenceRidley AJ, & Hall A ( 1992 ). Distinct patterns of actin organization regulated by the small GTP- binding proteins Rac and Rho. Cold Spring Harb Symp Quant Biol 57, 661 – 671.en_US
dc.identifier.citedreferenceSakaba T, & Neher E ( 2003 ). Involvement of actin polymerization in vesicle recruitment at the calyx of held synapse. J Neurosci 23, 837 – 846.en_US
dc.identifier.citedreferenceSelf AJ, Paterson HF & Hall A ( 1993 ). Different structural organization of Ras and Rho effector domains. Oncogene 8, 655 – 661.en_US
dc.identifier.citedreferenceShuang R, Zhang L, Fletcher A, Groblewski GE, Pevsner J & Stuenkel EL ( 1998 ). Regulation of Munc-18/syntaxin 1A interaction by cyclin-dependent kinase 5 in nerve endings. J Biol Chem 273, 4957 – 4966.en_US
dc.identifier.citedreferenceSontag JM, Aunis D & Bader MF ( 1988 ). Peripheral actin filaments control calcium-mediated catecholamine release from streptolysin-O-permeabilized chromaffin cells. Eur J Cell Biol 46, 316 – 326.en_US
dc.identifier.citedreferenceTapon N, Nagata K, Lamarche N & Hall A ( 1998 ). A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways. EMBO J 17, 1395 – 1404.en_US
dc.identifier.citedreferenceTchakarov LE, Zhang L, Rose SD, Tang R & Trifaro JM ( 1998 ). Light and electron microscopic study of changes in the organization of the cortical actin cytoskeleton during chromaffin cell secretion. J Histochem Cytochem 46, 193 – 203.en_US
dc.identifier.citedreferenceTolias KF, Cantley LC & Carpenter CL ( 1995 ). Rho family GTPases bind to phosphoinositide kinases. J Biol Chem 270, 17656 – 17659.en_US
dc.identifier.citedreferenceTrifaro JM, Rodriguez Del Castillo A & Vitale ML ( 1992a ). Dynamic changes in chromaffin cell cytoskeleton as prelude to exocytosis. Mol Neurobiol 6, 339 – 358.en_US
dc.identifier.citedreferenceTrifaro JM, & Vitale ML ( 1993 ). Cytoskeleton dynamics during neurotransmitter release. Trends Neurosci 16, 466 – 472.en_US
dc.identifier.citedreferenceTrifaro JM, Vitale ML & Rodriguez Del Castillo A ( 1992b ). Cytoskeleton and molecular mechanisms in neurotransmitter release by neurosecretory cells. Eur J Pharmacol 225, 83 – 104.en_US
dc.identifier.citedreferenceVitale ML, Rodriguez Del Castillo A, Tchakarov L & Trifaro JM ( 1991 ). Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. J Cell Biol 113, 1057 – 1067.en_US
dc.identifier.citedreferenceVitale ML, Seward EP & Trifaro JM ( 1995 ). Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353 – 363.en_US
dc.identifier.citedreferenceWick PF, Senter RA, Parsels LA, Uhler MD & Holz RW ( 1993 ). Transient transfection studies of secretion in bovine chromaffin cells and PC12 cells. Generation of kainate-sensitive chromaffin cells. J Biol Chem 268, 10983 – 10989.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Name:
jphysiol.2003.039073.pdf
Size:
641.0KB
Format:
PDF
View/Open

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.