<P><B>Summary</B></P><P>Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca<SUP>2+</SUP>-binding protein, S100A4, which causes enhanced cell migration and metastasis in c...
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https://www.riss.kr/link?id=A107759833
Elliott, Paul  ; R. ; Irvine, Andrew  ; F. ; Jung, Hyun  ; Suk ; Tozawa, Kaeko ; Pastok, Martyna  ; W. ; Picone, Remigio ; Badyal, Sandip  ; K. ; Basran, Jaswir ; Rudland, Philip  ; S. ; Barraclough, Roger ; Lian, Lu-Yun ; Bagshaw, Clive  ; R. ; Kriajevska, Marina ; Barsukov, Igor  ; L.
2012
-
SCOPUS,SCIE
학술저널
654-666(13쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<P><B>Summary</B></P><P>Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca<SUP>2+</SUP>-binding protein, S100A4, which causes enhanced cell migration and metastasis in c...
<P><B>Summary</B></P><P>Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca<SUP>2+</SUP>-binding protein, S100A4, which causes enhanced cell migration and metastasis in certain cancers. Our NMR structure shows that an S100A4 dimer binds to a single myosin heavy chain in an asymmetrical configuration. NMIIA in the complex forms a continuous helix that stretches across the surface of S100A4 and engages the Ca<SUP>2+</SUP>-dependent binding sites of each subunit in the dimer. Synergy between these sites leads to a very tight association (K<SUB>D</SUB> ∼1 nM) that is unique in the S100 family. Single-residue mutations that remove this synergy weaken binding and ameliorate the effects of S100A4 on NMIIA filament assembly and cell spreading in A431 human epithelial carcinoma cells. We propose a model for NMIIA filament disassembly by S100A4 in which initial binding to the unstructured NMIIA tail initiates unzipping of the coiled coil and disruption of filament packing.</P>