Show simple item record

Defined sequence segments of the small heat shock proteins HSP25 and αB-crystallin inhibit actin polymerization

dc.contributor.authorWieske, Martinen_US
dc.contributor.authorBenndorf, Raineren_US
dc.contributor.authorBehlke, Joachimen_US
dc.contributor.authorDölling, Rudolfen_US
dc.contributor.authorGrelle, Gerlindeen_US
dc.contributor.authorBielka, Heinzen_US
dc.contributor.authorLutsch, Gudrunen_US
dc.date.accessioned2010-04-01T14:49:08Z
dc.date.available2010-04-01T14:49:08Z
dc.date.issued2001-04-01en_US
dc.identifier.citationWieske, Martin; Benndorf, Rainer; Behlke, Joachim; DÖlling, Rudolf; Grelle, Gerlinde; Bielka, Heinz; Lutsch, Gudrun (2001). "Defined sequence segments of the small heat shock proteins HSP25 and αB-crystallin inhibit actin polymerization." European Journal of Biochemistry 268(7): 2083-2090. <http://hdl.handle.net/2027.42/65269>en_US
dc.identifier.issn0014-2956en_US
dc.identifier.issn1432-1033en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/65269
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11277931&dopt=citationen_US
dc.format.extent639764 bytes
dc.format.extent3110 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Science Ltden_US
dc.rightsFederation of European Biochemical Societiesen_US
dc.subject.otherActin Polymerizationen_US
dc.subject.otherElectron Microscopyen_US
dc.subject.otherFluorescence Spectroscopyen_US
dc.subject.otherSmall Heat Shock Proteinsen_US
dc.subject.otherPhosphorylation.en_US
dc.titleDefined sequence segments of the small heat shock proteins HSP25 and αB-crystallin inhibit actin polymerizationen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, USA;en_US
dc.contributor.affiliationotherMax DelbrÜck Center of Molecular Medicine, Berlin, Germany;en_US
dc.contributor.affiliationotherBiosyntan GmbH, Berlin-Buch, Germanyen_US
dc.identifier.pmid11277931en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/65269/1/j.1432-1327.2001.02082.x.pdf
dc.identifier.doi10.1046/j.1432-1327.2001.02082.xen_US
dc.identifier.sourceEuropean Journal of Biochemistryen_US
dc.identifier.citedreferenceIngolia, T.D. & Craig, E.A. ( 1982 ) Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl Acad. Sci. USA 79, 2360 – 2364.en_US
dc.identifier.citedreferenceKlemenz, R., FrÖhli, E., Steiger, R.H., SchÄfer, R., Aoyama, A. ( 1991 ) αB-crystallin is a small heat shock protein. Proc. Natl Acad. Sci. USA 88, 3652 – 3656.en_US
dc.identifier.citedreferenceArrigo, P. & Landry, J. ( 1994 ) Expression and function of the low-molecular-weight heat shock proteins. In The Biology of Heat Shock Proteins and Molecular Chaperones. ( Morimoto, R.I., Tissieres, A. & Georgopoulos, C., eds), pp. 335 – 373. Cold Spring Harbor Laboratory Press, Plainview, New York.en_US
dc.identifier.citedreferenceEhrnsperger, M., Buchner, J., Gaestel, M. ( 1997 ) Structure and function of small heat shock proteins. In Molecular Chaperones in the Life Cycle of Proteins. ( Fink, A.I. & Goto, S., eds), pp.  533 – 576. Marcel Dekker Inc, New York.en_US
dc.identifier.citedreferenceSiezen, R.J., Bindels, J.G., Hoenders, H.J. ( 1978 ) The quaternary structure of bovine α-crystallin. Eur. J. Biochem. 91, 387 – 396.en_US
dc.identifier.citedreferenceArrigo, A.P., Suhan, J.P., Welch, W.J. ( 1988 ) Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol. Cell. Biol. 8, 5059 – 5071.en_US
dc.identifier.citedreferenceBehlke, J., Lutsch, G., Gaestel, M., Bielka, H. ( 1991 ) Supramolecular structure of the recombinant small heat shock protein hsp25. FEBS Lett. 288, 119 – 122.en_US
dc.identifier.citedreferenceBenndorf, R., Hayess, K., Ryazantsev, S., Wieske, M., Behlke, J., Lutsch, G. ( 1994 ) Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J. Biol. Chem. 269, 20780 – 20784.en_US
dc.identifier.citedreferenceChiesa, R., Gawinowicz Kolks, M.A., Kleiman, N.J., Spector, A. ( 1987 ) The phosphorylation sites of the B 2 chain of bovine α-crystallin. Biochem. Biophys. Res. Commun. 144, 1340 – 1347.en_US
dc.identifier.citedreferenceVoorter, C.E., de Haard Hoekman, W.A., Roersma, E.S., Meyer, H.E., Bloemendal, H., de Jong, W.W. ( 1989 ) The in vivo phosphorylation sites of bovine αB-crystallin. FEBS Lett. 259, 50 – 52.en_US
dc.identifier.citedreferenceGaestel, M., SchrÖder, W., Benndorf, R., Lippmann, C., Buchner, K., Hucho, V.A., Erdmann, V., Bielka, H. ( 1991 ) Identification of the phosphorylation sites of the murine small heat shock protein hsp25. J. Biol. Chem. 266, 14721 – 14724.en_US
dc.identifier.citedreferenceLandry, J., Lambert, H., Zhou, M., Lavoie, J.N., Hickey, E., Weber, L.A., Anderson, C.W. ( 1992 ) Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J. Biol. Chem. 267, 794 – 803.en_US
dc.identifier.citedreferenceIto, H., Okamoto, K., Nakayama, H., Isobe, T., Kato, K. ( 1997 ) Phosphorylation of αB-crystallin in response to various types of stress. J. Biol. Chem. 272, 29934 – 29941.en_US
dc.identifier.citedreferenceHorwitz, J. ( 1992 ) α-Crystallin can function as a molecular chaperone. Proc. Natl Acad. Sci. USA 89, 10449 – 10453.en_US
dc.identifier.citedreferenceJakob, U., Gaestel, M., Engel, K., Buchner, J. ( 1993 ) Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517 – 1520.en_US
dc.identifier.citedreferenceChiesi, M., Longoni, S., Limbruno, U. ( 1990 ) Cardiac alpha-crystallin. III. Involvement during heart ischemia. Mol. Cell. Biochem. 97, 129 – 136.en_US
dc.identifier.citedreferenceBennardini, F., Wrzosek, A., Chiesi, M. ( 1992 ) αB-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ. Res. 71, 288 – 294.en_US
dc.identifier.citedreferenceNicholl, I.D. & Quinlan, R.A. ( 1994 ) Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J.   13, 945 – 953.en_US
dc.identifier.citedreferenceIwaki, T., Iwaki, A., Tateishi, J., Goldman, J.E. ( 1994 ) Sense and antisense modification of glial αB-crystallin production results in alterations of stress fiber formation and thermoresistence. J. Cell Biol. 125, 1385 – 1393.en_US
dc.identifier.citedreferenceWang, K. & Spector, A. ( 1996 ) α-Crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation-dependent manner. Eur. J. Biochem. 242, 56 – 66.en_US
dc.identifier.citedreferenceLutsch, G., Vetter, R., Offhauss, U., Wieske, M., GrÖne, H.J., Klemenz, R., Schimke, I., Stahl, J., Benndorf, R. ( 1997 ) Abundance and location of the small heat shock proteins HSP25 and αB-crystallin in rat and human heart. Circulation 96, 3466 – 3476.en_US
dc.identifier.citedreferenceMiron, T., Vancompernolle, K., Vandekerckhove, J., Wilchek, M., Geiger, B. ( 1991 ) A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J. Cell Biol. 114, 255 – 261.en_US
dc.identifier.citedreferenceRahman, D.R.J., Bentley, N.J., Tuite, M.F. ( 1995 ) The Saccharomyces cerevisiae small heat shock protein Hsp26 inhibits actin polymerization. Biochem. Soc. Trans. 23, 77S.en_US
dc.identifier.citedreferenceLavoie, J.N., Gingras-Breton, G., Tanguay, R.M., Landry, J. ( 1993 ) Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J. Biol. Chem. 268, 3420 – 3429.en_US
dc.identifier.citedreferenceLavoie, J.N., Hickey, E., Weber, L.A., Landry, J. ( 1993 ) Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. Biol. Chem. 268, 24210 – 24214.en_US
dc.identifier.citedreferenceWelsh, M.J., Wu, W., Parvinen, M., Gilmont, R.R. ( 1996 ) Variation in expression of hsp27 messenger ribonucleic acid during the cycle of the seminiferous epithelium and co-localization of hsp27 and microfilaments in Sertoli cells of the rat. Biol. Reprod. 55, 141 – 151.en_US
dc.identifier.citedreferencePiotrowicz, R.S. & Levin, E.G. ( 1997 ) Basolateral membrane-associated 27-kDa heat shock protein and microfilament polymerization. J. Biol. Chem. 272, 25920 – 25927.en_US
dc.identifier.citedreferencePiotrowicz, R.S., Hickey, E., Levin, E.G. ( 1998 ) Heat shock protein 27 kDa expression and phosphorylation regulates endothelial cell migration. FASEB J. 12, 1481 – 1490.en_US
dc.identifier.citedreferenceLoktionova, S.A. & Kabakov, A.E. ( 1998 ) Protein phosphatase inhibitors and heat preconditioning prevent Hsp27 dephosphorylation, F-actin disruption and deterioration of morphology in ATP-depleted endothelial cells. FEBS Lett. 433, 294 – 300.en_US
dc.identifier.citedreferenceSchneider, G.B., Hamano, H., Cooper, L.F. ( 1998 ) In vivo evaluation of hsp27 as an inhibitor of actin polymerization: Hsp27 limits actin stress fiber and focal adhesion formation after heat shock. J. Cell. Physiol. 177, 575 – 584.en_US
dc.identifier.citedreferenceGaestel, M., Gross, B., Benndorf, R., Strauss, M., Schunck, W.-H., Kraft, R., Otto, A., BÖhm, H., Stahl, J., Drabsch, H., Bielka, H. ( 1989 ) Molecular cloning, sequencing and expression in Escherichia coli of the 25-kDa growth-related protein of Ehrlich ascites tumor and its homology to mammalian stress proteins. Eur. J. Biochem. 179, 209 – 213.en_US
dc.identifier.citedreferenceAtherton, A. & Sheppard, R.C. ( 1989 ) Solid Phase Peptide Synthesis – a Practical Approach. IRL Press, Oxford.en_US
dc.identifier.citedreferenceKaras, M. & Hillenkamp, F. ( 1988 ) Laser desorption ionisation of proteins with molecular masses exceeding 10.000 daltons. Anal. Chem. 60, 2299 – 2301.en_US
dc.identifier.citedreferencePardee, J.D. & Spudich, J.A. ( 1982 ) Purification of muscle actin. Methods Enzymol. 85, 164 – 181.en_US
dc.identifier.citedreferencePollard, T.D. ( 1983 ) Measurement of rate constants for actin filament elongation in solution. Anal. Biochem. 134, 406 – 412.en_US
dc.identifier.citedreferenceKouyama, T. & Mihashi, K. ( 1981 ) Fluorimetry study of N -(1-pyrenyl) iodoacetamide-labelled F-actin. Eur. J. Biochem. 114, 33 – 38.en_US
dc.identifier.citedreferenceYonezawa, N., Nishida, E., Iida, K., Kumagai, H., Yahara, I., Sakai, H. ( 1991 ) Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin. J. Biol. Chem. 266, 10485 – 10489.en_US
dc.identifier.citedreferenceVancompernolle, K., Goethals, M., Huet, C., Louvard, D., Vandekerckhove, J. ( 1992 ) G- to F-actin modulation by single amino acid substitution in the actin binding site of actobindin and thymosin beta 4. EMBO J. 11, 4739 – 4746.en_US
dc.identifier.citedreferenceBresnick, A.R., Janmey, P.A., Condeelis, J. ( 1991 ) Evidence that a 27-residue sequence is the actin-binding site of ABP-120. J. Biol. Chem. 266, 12989 – 12993.en_US
dc.identifier.citedreferenceHug, C., Miller, T.M., Torres, M.A., Casella, J.F., Cooper, J.A. ( 1992 ) Identification and characterization of an actin-binding site of CapZ. J. Cell Biol. 116, 923 – 931.en_US
dc.identifier.citedreferenceTurunen, O., Sainio, M., JÄÄskelÄinen, J., Carpen, O., Vaheri, A. ( 1998 ) Structure-function relationships in the ezrin family and the effect of tumor-associated point mutations in neurofibromatosis 2 protein. Biochim. Biophys. Acta 1387, 1 – 16.en_US
dc.identifier.citedreferenceVancompernolle, K., Vandekerckhove, J., Bubb, M.R., Korn, E.D. ( 1991 ) The interfaces of actin and Acanthamoeba actobindin. Identification of a new actin-binding motif. J. Biol. Chem. 266, 15427 – 15431.en_US
dc.identifier.citedreferenceBrophy, C.M., Lamb, S., Graham, A. ( 1999 ) The small heat shock-related protein-20 is an actin-associated protein. J. Vasc. Surg. 29, 326 – 333.en_US
dc.identifier.citedreferenceKim, K.K., Kim, R., Kim, S.H. ( 1998 ) Crystal structure of a small heat-shock protein. Nature (Lond. ) 394, 595 – 599.en_US
dc.identifier.citedreferenceWelsh, M.J. & Gaestel, M. ( 1998 ) Small heat-shock protein family: function in health and disease. Ann. NY Acad. Sci. 851, 28 – 35.en_US
dc.identifier.citedreferenceSmoyer, W.E., Ransom, R., Harris, R.C., Welsh, M.J., Lutsch, G., Benndorf, R. ( 2000 ) Ischemic acute renal failure induces differential expression of small heat shock proteins. J. Am. Soc. Nephrol. 11, 211 – 221.en_US
dc.identifier.citedreferenceHuot, J., Houle, F., Spitz, D.R., Landry, J. ( 1996 ) HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res. 56, 273 – 279.en_US
dc.identifier.citedreferenceSchaefer, C., Clapp, P., Welsh, M.J., Benndorf, R., Williams, J.A. ( 1999 ) HSP27 expression regulates CCK-induced changes of the actin cytoskeleton in CHO-CCK-A cells. Am. J. Physiol. 277, C1032 – C1043.en_US
dc.identifier.citedreferenceLoktionova, S.A., Ilyinskaya, O.P., Kabakov, A.E. ( 1998 ) Early and delayed tolerance to simulated ischemia in heat-preconditioned endothelial cells: a role for HSP27. Am. J. Physiol. 275 ( Heart Circ. Physiol. 44 ), H2147 – H2158.en_US
dc.identifier.citedreferenceDel Vecchio, P., MacElroy, K., Rosser, M., Church, R. ( 1984 ) Association of α−crystallin with actin in cultured lens cells. Curr. Eye Res. 3, 1213 – 1219.en_US
dc.identifier.citedreferenceKato, K., Ito, H., Kamei, K., Inaguma, Y., Iwamoto, I., Saga, S. ( 1998 ) Phosphorylation of αB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J. Biol. Chem. 273, 28346 – 28354.en_US
dc.identifier.citedreferenceStokoe, D., Engel, K., Campbell, D.G., Cohen, P., Gaestel, M. ( 1992 ) Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small heat shock proteins. FEBS Lett. 313, 307 – 313.en_US
dc.identifier.citedreferenceVan den Ijssel, P.R.L.A., Overkamp, P., Bloemendal, H., de Jong, W.W. ( 1998 ) Phosphorylation of αB-crystallin and HSP27 is induced by similar stressors in HeLa cells. Biochem. Biophys. Res. Comm. 247, 518 – 523.en_US
dc.identifier.citedreferenceBÄhler, M. & Greengard, P. ( 1987 ) Synapsin I bundles F-actin in a phosphorylation-dependent manner. Nature (Lond. ) 326, 704 – 707.en_US
dc.identifier.citedreferenceYamashiro, S., Yamakita, Y., Ishikawa, R., Matsumura, F. ( 1990 ) Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilaments. Nature (Lond. ) 344, 675 – 678.en_US
dc.identifier.citedreferenceAgnew, B.J., Minamide, L.S., Bamburg, R.J. ( 1995 ) Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270, 17582 – 17587.en_US
dc.identifier.citedreferenceMoriyama, K., Iida, K., Yahara, I. ( 1996 ) Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1, 73 – 86.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

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.