| Structural highlights
Function
ACTNA_DICDI F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.[1] [2] [3] [4] [5] [6] [7] [8] MYH10_HUMAN Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9.[9] [10]
Publication Abstract from PubMed
We determined the crystal structure of the motor domain of human non-muscle myosin 2B (NM-2B) in a nucleotide-free state and at a resolution of 2.8A. The structure shows the motor domain with an open active site and the large cleft that divides the 50kDa domain in a closed state. Compared to other rigor-like myosin motor domain structures, our structure shows subtle but significant conformational changes in regions important for actin binding and mechanochemical coupling. Moreover, our crystal structure helps to rationalize the impact of myosin, heavy chain 9 (MYH9)-related disease mutations Arg709Cys and Arg709His on the kinetic and functional properties of NM-2B and of the closely related non-muscle myosin 2A (NM-2A).
Crystal structure of the rigor-like human non-muscle myosin-2 motor domain.,Munnich S, Pathan-Chhatbar S, Manstein DJ FEBS Lett. 2014 Dec 20;588(24):4754-60. doi: 10.1016/j.febslet.2014.11.007. Epub , 2014 Nov 15. PMID:25451231[11]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weber I. Computer-assisted morphometry of cell-substratum contacts. Croat Med J. 1999 Sep;40(3):334-9. PMID:10411959
- ↑ Rivero F, Furukawa R, Fechheimer M, Noegel AA. Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium. J Cell Sci. 1999 Aug;112 ( Pt 16):2737-51. PMID:10413681
- ↑ Ponte E, Rivero F, Fechheimer M, Noegel A, Bozzaro S. Severe developmental defects in Dictyostelium null mutants for actin-binding proteins. Mech Dev. 2000 Mar 1;91(1-2):153-61. doi: 10.1016/s0925-4773(99)00292-0. PMID:10704840 doi:https://dx.doi.org/10.1016/s0925-4773(99)00292-0
- ↑ Witke W, Schleicher M, Noegel AA. Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell. 1992 Jan 10;68(1):53-62. PMID:1732064
- ↑ Wallraff E, Schleicher M, Modersitzki M, Rieger D, Isenberg G, Gerisch G. Selection of Dictyostelium mutants defective in cytoskeletal proteins: use of an antibody that binds to the ends of alpha-actinin rods. EMBO J. 1986 Jan;5(1):61-7. PMID:3956480
- ↑ Condeelis J, Vahey M, Carboni JM, DeMey J, Ogihara S. Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix. J Cell Biol. 1984 Jul;99(1 Pt 2):119s-126s. PMID:6746725
- ↑ Witke W, Hofmann A, Koppel B, Schleicher M, Noegel AA. The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis. J Cell Biol. 1993 May;121(3):599-606. PMID:8486739
- ↑ Rivero F, Koppel B, Peracino B, Bozzaro S, Siegert F, Weijer CJ, Schleicher M, Albrecht R, Noegel AA. The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J Cell Sci. 1996 Nov;109 ( Pt 11):2679-91. PMID:8937986
- ↑ Betapudi V. Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading. PLoS One. 2010 Jan 5;5(1):e8560. doi: 10.1371/journal.pone.0008560. PMID:20052411 doi:https://dx.doi.org/10.1371/journal.pone.0008560
- ↑ Cai L, Fritz D, Stefanovic L, Stefanovic B. Nonmuscle myosin-dependent synthesis of type I collagen. J Mol Biol. 2010 Aug 27;401(4):564-78. doi: 10.1016/j.jmb.2010.06.057. Epub 2010 , Jul 13. PMID:20603131 doi:https://dx.doi.org/10.1016/j.jmb.2010.06.057
- ↑ Munnich S, Pathan-Chhatbar S, Manstein DJ. Crystal structure of the rigor-like human non-muscle myosin-2 motor domain. FEBS Lett. 2014 Dec 20;588(24):4754-60. doi: 10.1016/j.febslet.2014.11.007. Epub , 2014 Nov 15. PMID:25451231 doi:https://dx.doi.org/10.1016/j.febslet.2014.11.007
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