Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence

Unger A, Brunne B, Hinssen H (2013)
Archives Of Biochemistry And Biophysics 536(1): 38-45.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Unger, Andreas; Brunne, Bianka; Hinssen, HorstUniBi
Abstract / Bemerkung
Two distinct isoforms of the Ca-dependent actin filament severing protein gelsolin were identified in cross-striated muscles of the American lobster. The variants (termed LG1 and LG2) differ by an extension of 18 AA at the C-terminus of LG1, and by two substitutions at AA735 and AA736, the two C-terminal amino acids of LG2. Functional comparison of the isolated and purified proteins revealed gelsolin-typical properties for both with differences in Ca2+-sensitivity, LG2 being activated at significant lower Ca-concentration than LG1: Half maximal activation for both filament severing and G-actin binding was similar to 4 x 10(-7) M Ca2+ for LG2 vs. similar to 2 x 10(-6) M Ca2+ for LG1. This indicates a differential activation for the two isoproteins in vivo where they are present in almost equal amounts in the muscle cell. Structure prediction modeling on the basis of the known structure of mammalian gelsolin shows that LG2 lacks the C-terminal alpha-helix which is involved in contact formation between domains G6 and G2. In both mammalian gelsolin and LG1, this "latch bridge" is assumed to play a critical role in Ca2+-activation by keeping gelsolin in a closed, inactive conformation at low [Ca2+]. In LG2, the reduced contact between G6 and G2 may be responsible for its activation at low Ca2+-concentration. (C) 2013 Elsevier Inc. All rights reserved.
Actin filaments; Actin-binding proteins; Isoforms; Gelsolin; Lobster; Calcium-dependence; striated muscle
Archives Of Biochemistry And Biophysics
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Unger A, Brunne B, Hinssen H. Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence. Archives Of Biochemistry And Biophysics. 2013;536(1):38-45.
Unger, A., Brunne, B., & Hinssen, H. (2013). Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence. Archives Of Biochemistry And Biophysics, 536(1), 38-45. doi:10.1016/
Unger, A., Brunne, B., and Hinssen, H. (2013). Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence. Archives Of Biochemistry And Biophysics 536, 38-45.
Unger, A., Brunne, B., & Hinssen, H., 2013. Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence. Archives Of Biochemistry And Biophysics, 536(1), p 38-45.
A. Unger, B. Brunne, and H. Hinssen, “Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence”, Archives Of Biochemistry And Biophysics, vol. 536, 2013, pp. 38-45.
Unger, A., Brunne, B., Hinssen, H.: Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence. Archives Of Biochemistry And Biophysics. 536, 38-45 (2013).
Unger, Andreas, Brunne, Bianka, and Hinssen, Horst. “Isoforms of gelsolin from lobster striated muscles differ in Calcium-dependence”. Archives Of Biochemistry And Biophysics 536.1 (2013): 38-45.

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Four paralog gelsolin genes are differentially expressed in the earthworm Lumbricus terrestris.
Thiruketheeswaran P, Thomalla P, Krüger E, Hinssen H, D'Haese J., Comp Biochem Physiol B Biochem Mol Biol 208-209(), 2017
PMID: 28400331

50 References

Daten bereitgestellt von Europe PubMed Central.

Gelsolin superfamily proteins: key regulators of cellular functions.
Silacci P, Mazzolai L, Gauci C, Stergiopulos N, Yin HL, Hayoz D., Cell. Mol. Life Sci. 61(19-20), 2004
PMID: 15526166
Multifunctional roles of gelsolin in health and diseases.
Li GH, Arora PD, Chen Y, McCulloch CA, Liu P., Med Res Rev 32(5), 2010
PMID: 22886630
Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.
Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL., Nature 323(6087), 1986
PMID: 3020431
The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.
Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC., Cell 90(4), 1997
PMID: 9288746
Fragmin: a calcium ion sensitive regulatory factor on the formation of actin filaments.
Hasegawa T, Takahashi S, Hayashi H, Hatano S., Biochemistry 19(12), 1980
PMID: 6893158

D’Haese, J. Comp. Physiol. 248(), 1987
Functional characteristics and the complete primary structure of ascidian gelsolin.
Ohtsuka Y, Nakae H, Abe H, Obinata T., Biochim. Biophys. Acta 1383(2), 1998
PMID: 9602133
Cloning of a secretory gelsolin from Drosophila melanogaster.
Heintzelman MB, Frankel SA, Artavanis-Tsakonas S, Mooseker MS., J. Mol. Biol. 230(3), 1993
PMID: 8386771
Identification of secreted and cytosolic gelsolin in Drosophila.
Stella MC, Schauerte H, Straub KL, Leptin M., J. Cell Biol. 125(3), 1994
PMID: 8175883
A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.
Luck A, D'Haese J, Hinssen H., Biochem. J. 305 ( Pt 3)(), 1995
PMID: 7848275
A novel gelsolin isoform expressed by oligodendrocytes in the central nervous system.
Vouyiouklis DA, Brophy PJ., J. Neurochem. 69(3), 1997
PMID: 9282921
C-terminally deleted fragments of 40-kDa earthworm actin modulator still show gelsolin activities.
Giebing T, Obermann WM, Furst D, D'Haese J., FEBS Lett. 417(2), 1997
PMID: 9395293
The complete sequence of a 40-kDa actin-modulating protein from the earthworm Lumbricus terrestris.
Giebing T, Hinssen H, D'Haese J., Eur. J. Biochem. 225(3), 1994
PMID: 7957213
Molecular cloning, over-expression, developmental regulation and immunolocalization of fragminP, a gelsolin-related actin-binding protein from Physarum polycephalum plasmodia.
T'Jampens D, Meerschaert K, Constantin B, Bailey J, Cook LJ, De Corte V, De Mol H, Goethals M, Van Damme J, Vandekerckhove J, Gettemans J., J. Cell. Sci. 110 ( Pt 10)(), 1997
PMID: 9191045
Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association.
MacLean-Fletcher S, Pollard TD., Biochem. Biophys. Res. Commun. 96(1), 1980
PMID: 6893667

Arnold, Bioinformatics 22(), 2006
Electron-microscopical localization of gelsolin in various crustacean muscles.
Unger A, Hinssen H., Cell Tissue Res. 341(2), 2010
PMID: 20607291
Isolation and properties of two actin-binding domains in gelsolin.
Kwiatkowski DJ, Janmey PA, Mole JE, Yin HL., J. Biol. Chem. 260(28), 1985
PMID: 2999108
Involvement of a gelsolin-related protein in spermatogenesis of the earthworm Lumbricus terrestris.
Kruger E, Hinssen H, D'Haese J., Cell Tissue Res. 332(1), 2008
PMID: 18197420
Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein.
Rodriguez Del Castillo A, Lemaire S, Tchakarov L, Jeyapragasan M, Doucet JP, Vitale ML, Trifaro JM., EMBO J. 9(1), 1990
PMID: 2153078
Identification of critical functional and regulatory domains in gelsolin.
Kwiatkowski DJ, Janmey PA, Yin HL., J. Cell Biol. 108(5), 1989
PMID: 2541138
Ca2+ regulation of gelsolin by its C-terminal tail.
Lin KM, Mejillano M, Yin HL., J. Biol. Chem. 275(36), 2000
PMID: 10862770
Calcium regulation of gelsolin and adseverin: a natural test of the helix latch hypothesis.
Lueck A, Yin HL, Kwiatkowski DJ, Allen PG., Biochemistry 39(18), 2000
PMID: 10819996
The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.
Chumnarnsilpa S, Lee WL, Nag S, Kannan B, Larsson M, Burtnick LD, Robinson RC., Proc. Natl. Acad. Sci. U.S.A. 106(33), 2009
PMID: 19666531

Patkowski, Biopolymers 30(), 1990
Domain movement in gelsolin: a calcium-activated switch.
Robinson RC, Mejillano M, Le VP, Burtnick LD, Yin HL, Choe S., Science 286(5446), 1999
PMID: 10583954
Global structure changes associated with Ca2+ activation of full-length human plasma gelsolin.
Ashish , Paine MS, Perryman PB, Yang L, Yin HL, Krueger JK., J. Biol. Chem. 282(35), 2007
PMID: 17604278
Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin.
Narayan K, Chumnarnsilpa S, Choe H, Irobi E, Urosev D, Lindberg U, Schutt CE, Burtnick LD, Robinson RC., FEBS Lett. 552(2-3), 2003
PMID: 14527664
The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex.
Choe H, Burtnick LD, Mejillano M, Yin HL, Robinson RC, Choe S., J. Mol. Biol. 324(4), 2002
PMID: 12460571
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF.
Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC., EMBO J. 23(14), 2004
PMID: 15215896

Nag, Proc. Natl. Acad. Sci. USA 106(), 2009
Muscle gelsolin: isolation from heart tissue and characterization as an integral myofibrillar protein.
Rouayrenc JF, Fattoum A, Gabrion J, Audemard E, Kassab R., FEBS Lett. 167(1), 1984
PMID: 6321238

Clapham, Calcium signaling Cell 131(), 2007
Dynamic regulation of sarcomeric actin filaments in striated muscle.
Ono S., Cytoskeleton (Hoboken) 67(11), 2010
PMID: 20737540
Comparison of turnover of several myofibrillar proteins and critical evaluation of double isotope method.
Zak R, Martin AF, Prior G, Rabinowitz M., J. Biol. Chem. 252(10), 1977
PMID: 863889
Studies on actin. III. G-F transformation of actin and muscular contraction (experiments in vivo).
MARTONOSI A, GOUVEA MA, GERGELY J., J. Biol. Chem. 235(), 1960
PMID: 14421877
Incorporation of fluorescently labeled actin and tropomyosin into muscle cells.
Dome JS, Mittal B, Pochapin MB, Sanger JM, Sanger JW., Cell Differ. 23(1-2), 1988
PMID: 2453294
Incorporation of fluorescently labeled contractile proteins into freshly isolated living adult cardiac myocytes.
LoRusso SM, Imanaka-Yoshida K, Shuman H, Sanger JM, Sanger JW., Cell Motil. Cytoskeleton 21(2), 1992
PMID: 1559262
Contractility-dependent actin dynamics in cardiomyocyte sarcomeres.
Skwarek-Maruszewska A, Hotulainen P, Mattila PK, Lappalainen P., J. Cell. Sci. 122(Pt 12), 2009
PMID: 19470580


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