Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins

Khaitlina S, Hinssen H (2008)
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 477(2): 279-284.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
;
Abstract / Bemerkung
The polymerization of scallop p-like actin is significantly slower than that of skeletal muscle alpha-actin. To reveal which steps of polymerization contribute to this difference, we estimated the efficiency of nucleation of the two actins, the rates of filament elongation at spontaneous and gelsolin-nucleated polymerization and the turnover rates of the filament Subunits at steady-state. Scallop actin nucleated nearly twice less efficient than rabbit actin. In actin filaments with free ends, when dynamics at the barbed ends overrides that at the pointed ends, the relative association rate constants of alpha- and beta-actin were similar, whereas the relative dissociation rate constant of beta-ATP-actin subunits was 2- to 3-fold higher than that of alpha-actin. The 2- to 3-fold faster polymerization of skeletal muscle versus scallop Ca-actin was preserved with gelsolin-capped actin filaments when only polymerization at the pointed end is possible. With gelsolin-induced polymerization, the rate constants of dissociation of ATP-actin subunits from the pointed ends were similar, while the association rate constant of beta-actin to the pointed filament ends was twice lower than that of alpha-actin. This difference may be of physiological relevance for functional intracellular sorting of actin isoforms. (C) 2008 Elsevier Inc. All rights reserved.
Erscheinungsjahr
Zeitschriftentitel
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Band
477
Ausgabe
2
Seite(n)
279-284
ISSN
PUB-ID

Zitieren

Khaitlina S, Hinssen H. Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. 2008;477(2):279-284.
Khaitlina, S., & Hinssen, H. (2008). Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 477(2), 279-284. doi:10.1016/j.abb.2008.06.016
Khaitlina, S., and Hinssen, H. (2008). Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 477, 279-284.
Khaitlina, S., & Hinssen, H., 2008. Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 477(2), p 279-284.
S. Khaitlina and H. Hinssen, “Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins”, ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, vol. 477, 2008, pp. 279-284.
Khaitlina, S., Hinssen, H.: Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS. 477, 279-284 (2008).
Khaitlina, Sofia, and Hinssen, Horst. “Difference in polymerization and steady-state dynamics of free and gelsolin-capped filaments formed by alpha- and beta-isoactins”. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 477.2 (2008): 279-284.

4 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Cooperative effects of tropomyosin on the dynamics of the actin filament.
Khaitlina S, Tsaplina O, Hinssen H., FEBS Lett 591(13), 2017
PMID: 28555876
Actin isoforms and reorganization of adhesion junctions in epithelial-to-mesenchymal transition of cervical carcinoma cells.
Shagieva GS, Domnina LV, Chipysheva TA, Ermilova VD, Chaponnier C, Dugina VB., Biochemistry (Mosc) 77(11), 2012
PMID: 23240564
The in vitro motility assay parameters of actin filaments from Mytilus edulis exposed in vivo to copper ions.
Vikhoreva NN, Vikhorev PG, Fedorova MA, Hoffmann R, Månsson A, Kuleva NV., Arch Biochem Biophys 491(1-2), 2009
PMID: 19796626

56 References

Daten bereitgestellt von Europe PubMed Central.

The functional importance of multiple actin isoforms.
Rubenstein PA., Bioessays 12(7), 1990
PMID: 2203335
Actin isoforms.
Herman IM., Curr. Opin. Cell Biol. 5(1), 1993
PMID: 8448030
Isoform sorting and the creation of intracellular compartments.
Gunning P, Weinberger R, Jeffrey P, Hardeman E., Annu. Rev. Cell Dev. Biol. 14(), 1998
PMID: 9891787
Functional specificity of actin isoforms.
Khaitlina SY., Int. Rev. Cytol. 202(), 2001
PMID: 11061563
Medical aspects of the actin cytoskeleton.
Janmey PA, Chaponnier C., Curr. Opin. Cell Biol. 7(1), 1995
PMID: 7755982
Pathological situations characterized by altered actin isoform expression.
Chaponnier C, Gabbiani G., J. Pathol. 204(4), 2004
PMID: 15495226
Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function.
von Arx P, Bantle S, Soldati T, Perriard JC., J. Cell Biol. 131(6 Pt 2), 1995
PMID: 8557743
Functional nonequivalence of Drosophila actin isoforms.
Fyrberg EA, Fyrberg CC, Biggs JR, Saville D, Beall CJ, Ketchum A., Biochem. Genet. 36(7-8), 1998
PMID: 9791722
Chick cytoplasmic actin and muscle actin have different structural genes.
Storti RV, Rich A., Proc. Natl. Acad. Sci. U.S.A. 73(7), 1976
PMID: 1065885
Structural compartments within neurons: developmentally regulated organization of microfilament isoform mRNA and protein.
Hannan AJ, Gunning P, Jeffrey PL, Weinberger RP., Mol. Cell. Neurosci. 11(5-6), 1998
PMID: 9698395
Determinants of mRNA localization.
Kislauskis EH, Singer RH., Curr. Opin. Cell Biol. 4(6), 1992
PMID: 1485968
beta-Actin messenger RNA localization and protein synthesis augment cell motility.
Kislauskis EH, Zhu X, Singer RH., J. Cell Biol. 136(6), 1997
PMID: 9087442
Spatial regulation of beta-actin translation by Src-dependent phosphorylation of ZBP1.
Huttelmaier S, Zenklusen D, Lederer M, Dictenberg J, Lorenz M, Meng X, Bassell GJ, Condeelis J, Singer RH., Nature 438(7067), 2005
PMID: 16306994
Beta and gamma actin mRNAs are differentially located within myoblasts.
Hill MA, Gunning P., J. Cell Biol. 122(4), 1993
PMID: 8349732

Khaitlina, Byokhimiya 41(), 1976
Polymerization of beta-like actin from scallop adductor muscle.
Khaitlina SYu ., FEBS Lett. 198(2), 1986
PMID: 3956731
Structural and functional variations in skeletal-muscle and scallop muscle actins.
Hue HK, Labbe JP, Harricane MC, Cavadore JC, Benyamin Y, Roustan C., Biochem. J. 256(3), 1988
PMID: 2464998
Correlation between polymerizability and conformation in scallop beta-like actin and rabbit skeletal muscle alpha-actin.
Khaitlina S, Antropova O, Kuznetsova I, Turoverov K, Collins JH., Arch. Biochem. Biophys. 368(1), 1999
PMID: 10415117
Comparative biochemistry of non-muscle actins.
Gordon DJ, Boyer JL, Korn ED., J. Biol. Chem. 252(22), 1977
PMID: 144137
Isolation and characterization of actin from cultured BHK cells.
Koffer A, Dickens MJ., J. Muscle Res. Cell. Motil. 8(5), 1987
PMID: 3429641
Effect of the substitution of muscle actin-specific subdomain 1 and 2 residues in yeast actin on actin function.
McKane M, Wen KK, Meyer A, Rubenstein PA., J. Biol. Chem. 281(40), 2006
PMID: 16882670
Biochemical characterization of ezrin-actin interaction.
Yao X, Cheng L, Forte JG., J. Biol. Chem. 271(12), 1996
PMID: 8636161
Utrophin actin binding domain: analysis of actin binding and cellular targeting.
Winder SJ, Hemmings L, Maciver SK, Bolton SJ, Tinsley JM, Davies KE, Critchley DR, Kendrick-Jones J., J. Cell. Sci. 108 ( Pt 1)(), 1995
PMID: 7738117
Arginylation of beta-actin regulates actin cytoskeleton and cell motility.
Karakozova M, Kozak M, Wong CC, Bailey AO, Yates JR 3rd, Mogilner A, Zebroski H, Kashina A., Science 313(5784), 2006
PMID: 16794040
Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary.
Johansson M, Lundberg M., BMC Biochem. 8(), 2007
PMID: 18070357

Margulis, Biophysika 27(), 1982
A Ca2+-dependent actin modulator from vertebrate smooth muscle.
Hinssen H, Small JV, Sobieszek A., FEBS Lett. 166(1), 1984
PMID: 6537923

AUTHOR UNKNOWN, 0
Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state.
Carlier MF, Pantaloni D, Korn ED., J. Biol. Chem. 259(16), 1984
PMID: 6236218

Carlier, J. Biol. Chem. 261(), 1984
Role of the DNase-I-binding loop in dynamic properties of actin filament.
Khaitlina SY, Strzelecka-Golaszewska H., Biophys. J. 82(1 Pt 1), 2002
PMID: 11751319
Control of actin assembly dynamics in cell motility.
Carlier MF, Pantaloni D., J. Biol. Chem. 282(32), 2007
PMID: 17576764
Ca-dependent binding of actin to gelsolin.
Khaitlina S, Hinssen H., FEBS Lett. 521(1-3), 2002
PMID: 12067717
Phalloidin binding and rheological differences among actin isoforms.
Allen PG, Shuster CB, Kas J, Chaponnier C, Janmey PA, Herman IM., Biochemistry 35(45), 1996
PMID: 8916891
Structural dynamics of F-actin: II. Cooperativity in structural transitions.
Orlova A, Prochniewicz E, Egelman EH., J. Mol. Biol. 245(5), 1995
PMID: 7844829
The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin.
Rybakova IN, Patel JR, Ervasti JM., J. Cell Biol. 150(5), 2000
PMID: 10974007
Sorting of actin isoforms in chicken auditory hair cells.
Hofer D, Ness W, Drenckhahn D., J. Cell. Sci. 110 ( Pt 6)(), 1997
PMID: 9099950
Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.
Prassler J, Stocker S, Marriott G, Heidecker M, Kellermann J, Gerisch G., Mol. Biol. Cell 8(1), 1997
PMID: 9017597
Arf6 modulates the beta-actin specific capping protein, betacap73.
Welch AY, Riley KN, D'Souza-Schorey C, Herman IM., Meth. Enzymol. 404(), 2005
PMID: 16413284

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 18619940
PubMed | Europe PMC

Suchen in

Google Scholar