TY - CHAP
T1 - Tropomyosins regulate the impact of actin binding proteins on actin filaments
AU - Lindberg, Uno
AU - Schutt, Clarence E.
AU - Goldman, Robert D.
AU - Nyåkern-Meazza, Maria
AU - Hillberg, Louise
AU - Rathje, Li Sophie Zhao
AU - Grenklo, Staffan
PY - 2008
Y1 - 2008
N2 - The state of actin depends intimately on its interaction partners in eukaryotic cells. Classically, the cooperative force-generating acto-myosin couple is turned off and on by the calcium-dependent binding and release of tropomyosin molecules. The situation with nonmuscle cells appears to be much more complicated, with tropomyosin isoforms regulating the kinds of tension-producing and stress-bearing structures formed of actin filaments. The polymerization of even the shortest gelsolin-capped filaments is efficiently promoted by the binding of tropomyosin, for example, a process that might occur all the way out to the leading edges of advancing cells. Recently, multimers of tropomyosin have been discovered that appear to be assembly intermediates, formed from identical tropomyosin molecules, which act as ready pools of tropomyosin during the catalytic formation of lamellipodia and filopodia. Remarkably, these multimers apparently reform during the disassembly of cellular actin-containing structures. The existence of these recyclable, tropomyosin isoform-specific structures suggests how cells prevent nonproductive association of non-identical, but closely similar, tropomyosin isoforms.
AB - The state of actin depends intimately on its interaction partners in eukaryotic cells. Classically, the cooperative force-generating acto-myosin couple is turned off and on by the calcium-dependent binding and release of tropomyosin molecules. The situation with nonmuscle cells appears to be much more complicated, with tropomyosin isoforms regulating the kinds of tension-producing and stress-bearing structures formed of actin filaments. The polymerization of even the shortest gelsolin-capped filaments is efficiently promoted by the binding of tropomyosin, for example, a process that might occur all the way out to the leading edges of advancing cells. Recently, multimers of tropomyosin have been discovered that appear to be assembly intermediates, formed from identical tropomyosin molecules, which act as ready pools of tropomyosin during the catalytic formation of lamellipodia and filopodia. Remarkably, these multimers apparently reform during the disassembly of cellular actin-containing structures. The existence of these recyclable, tropomyosin isoform-specific structures suggests how cells prevent nonproductive association of non-identical, but closely similar, tropomyosin isoforms.
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U2 - 10.1007/978-0-387-85766-4_17
DO - 10.1007/978-0-387-85766-4_17
M3 - Chapter
C2 - 19209825
AN - SCOPUS:60849125441
SN - 9780387857657
T3 - Advances in Experimental Medicine and Biology
SP - 223
EP - 231
BT - Tropomyosin
A2 - Gunning, Peter
ER -