Emerging complex pathways of the actomyosin powerstroke.
Actomyosin powers muscle contraction and various cellular activities, including cell division, differentiation, intracellular transport and sensory functions. Despite their crucial roles, key aspects of force generation have remained elusive. To perform efficient force generation, the powerstroke must occur while myosin is bound to actin. Paradoxically, this process must be initiated when myosin is in a very low actin-affinity state. Recent results shed light on a kinetic pathway selection mechanism whereby the actin-induced activation of the swing of myosin's lever enables efficient mechanical functioning. Structural elements and biochemical principles involved in this mechanism are conserved among various NTPase-effector (e.g. kinesin-microtubule, G protein exchange factor and kinase-scaffold protein) systems that perform chemomechanical or signal transduction.
Málnási-Csizmadia
András
A
Department of Biochemistry, Eötvös University, Pázmány P. stny. 1/C, H-1117 Budapest, Hungary. malna@elte.hu
Kovács
Mihály
M
D000205:Actomyosin / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D006801:Humans; D009119:Muscle Contraction; D009711:Nucleotides / Q000378:metabolism
D009711:Nucleotides; D000205:Actomyosin
Biochemistry. 1971 Dec 7;10(25):4617-24
4258719
EMBO J. 2007 Jan 10;26(1):265-74
17213877
Structure. 2005 Jan;13(1):131-41
15642268
Philos Trans R Soc Lond B Biol Sci. 2004 Dec 29;359(1452):1867-77
15647162
J Physiol. 2005 Mar 15;563(Pt 3):671-87
15611023
J Biol Chem. 2002 Jul 5;277(27):24114-9
11959853
J Biol Chem. 2008 Mar 28;283(13):8153-63
18211892
Nature. 1990 Sep 6;347(6288):37-44
2395459
Genome Biol. 2007;8(9):R196
17877792
Philos Trans R Soc Lond B Biol Sci. 2004 Dec 29;359(1452):1819-28
15647158
Annu Rev Biophys. 2010;39:539-57
20192767
Curr Opin Cell Biol. 2004 Feb;16(1):61-7
15037306
Science. 1993 Jul 2;261(5117):50-8
8316857
Nature. 1954 May 22;173(4412):971-3
13165697
Nature. 1954 May 22;173(4412):973-6
13165698
Biophys J. 1991 Feb;59(2):329-42
2009356
J Cell Biol. 1996 Oct;135(2):291-302
8896589
Trends Biochem Sci. 2000 Dec;25(12):607-11
11116187
Proc Natl Acad Sci U S A. 2010 Apr 13;107(15):6799-804
20351242
Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10482-6
7479824
J Biol Chem. 2000 Dec 8;275(49):38494-9
10954715
Mol Cell. 2007 Jan 12;25(1):141-9
17218277
Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):9994-9
17548820
Structure. 2007 May;15(5):553-64
17502101
Adv Protein Chem. 2005;71:161-93
16230112
Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11238-43
11016966
Science. 2006 Feb 10;311(5762):822-6
16424299
Biochemistry. 1995 Jul 18;34(28):8960-72
7619795
J Biol Chem. 2008 Dec 5;283(49):34121-8
18854311
Nat Cell Biol. 2003 Nov;5(11):980-6
14578909
Biophys J. 2005 Nov;89(5):L34-6
16169988
Nature. 2003 Sep 25;425(6956):419-23
14508494
Biochem J. 1974 Aug;141(2):331-49
4281653
J Muscle Res Cell Motil. 1998 Nov;19(8):877-86
10047987
Biochem J. 1974 Aug;141(2):351-64
4281654
EMBO J. 2004 Nov 24;23(23):4527-37
15510214
Proc Natl Acad Sci U S A. 2009 Apr 14;106(15):6140-5
19325123
Biophys J. 2009 May 6;96(9):3673-81
19413972
Proc Natl Acad Sci U S A. 2005 May 10;102(19):6873-8
15863618
Biophys J. 2008 Dec 15;95(12):5798-808
18835889
J Physiol. 1992;451:247-78
1403812
Ann Biomed Eng. 2008 Oct;36(10):1624-40
18642081
Nat Cell Biol. 2005 Sep;7(9):861-9
16100513
Nat Struct Biol. 2003 Oct;10(10):831-5
14502269
Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4459-64
8633089
Biochemistry. 2004 Dec 14;43(49):15404-17
15581352
Eur Biophys J. 2002 Jul;31(4):268-74
12122473
Cell. 2004 Mar 5;116(5):737-49
15006355
Biophys J. 2008 Oct;95(7):3322-9
18599626
Hung Acta Physiol. 1949;2(1-4):120-33
15397948
Nature. 2003 Sep 25;425(6956):423-7
14508495