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  Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3

Taft, M. H., Behrmann, E., Munske-Weidemann, L. C., Thiel, C., Raunser, S., & Manstein, D. J. (2013). Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3. The Journal of biological chemistry, 288(42), 30029-41. doi:10.1074/jbc.M113.497180.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-6386-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-6387-8
Genre: Journal Article

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 Creators:
Taft, M. H., Author
Behrmann, E.1, Author
Munske-Weidemann, L. C., Author
Thiel, C., Author
Raunser, S., Author
Manstein, D. J., Author
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1External Organizations, ou_persistent22              

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Free keywords: Actins/*chemistry/genetics/metabolism Adenosine Triphosphate/chemistry/genetics/metabolism Animals Binding Sites Cytoskeleton/chemistry/genetics/metabolism Drosophila melanogaster Humans Membrane Proteins/*chemistry/genetics/metabolism Mice Myosins/*chemistry/genetics/metabolism Protein Binding Rabbits Recombinant Proteins/chemistry/genetics/metabolism
 Abstract: Molecular motors of the myosin superfamily share a generic motor domain region. They commonly bind actin in an ATP-sensitive manner, exhibit actin-activated ATPase activity, and generate force and movement in this interaction. Class-18 myosins form heavy chain dimers and contain protein interaction domains located at their unique N-terminal extension. Here, we characterized human myosin-18A molecular function in the interaction with nucleotides, F-actin, and its putative binding partner, the Golgi-associated phosphoprotein GOLPH3. We show that myosin-18A comprises two actin binding sites. One is located in the KE-rich region at the start of the N-terminal extension and appears to mediate ATP-independent binding to F-actin. The second actin-binding site resides in the generic motor domain and is regulated by nucleotide binding in the absence of intrinsic ATP hydrolysis competence. This core motor domain displays its highest actin affinity in the ADP state. Electron micrographs of myosin-18A motor domain-decorated F-actin filaments show a periodic binding pattern independent of the nucleotide state. We show that the PDZ module mediates direct binding of myosin-18A to GOLPH3, and this interaction in turn modulates the actin binding properties of the N-terminal extension. Thus, myosin-18A can act as an actin cross-linker with multiple regulatory modulators that targets interacting proteins or complexes to the actin-based cytoskeleton.

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 Dates: 2013
 Publication Status: Published in print
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 Identifiers: Other: 23990465
DOI: 10.1074/jbc.M113.497180
ISSN: 1083-351X (Electronic)
ISSN: 0021-9258 (Linking)
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Title: The Journal of biological chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 288 (42) Sequence Number: - Start / End Page: 30029 - 41 Identifier: -