Structural Insights into Functional Overlapping and Differentiation among Myosin V Motors
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| Authors: | Andrey F. Z. Nascimento Daniel M. Trindade Celisa C. C. Tonoli Priscila O. de Giuseppe Leandro H. P. Assis Rodrigo V. Honorato Paulo S. L. de Oliveira Pravin Mahajan Nicola A. Burgess-Brown Frank von Delft Roy E. Larson Mario T. Murakami |
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| Affiliation: | From the ‡Brazilian Biosciences National Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo 13083-100, Brazil.;the §Structural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom, and ;the ¶Department of Cellular & Molecular Biology, Ribeirão Preto Medical School, University of São Paulo, São Paulo 14049-900, Brazil |
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| Abstract: | Myosin V (MyoV) motors have been implicated in the intracellular transport of diverse cargoes including vesicles, organelles, RNA-protein complexes, and regulatory proteins. Here, we have solved the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb, and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process, which is unique for the MyoVc subclass. Moreover, the cargo- and motor-binding sites were structurally assigned, indicating the conservation of residues involved in the recognition of adaptors for peroxisome transport and providing high resolution insights into motor domain inhibition by CBD. These results contribute to understanding the structural requirements for cargo transport, autoinhibition, and regulatory mechanisms in myosin V motors. |
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| Keywords: | Cell Signaling Crystal Structure Intracellular Trafficking Molecular Motors Myosin Myosin V Cargo-binding Domain Molecular Plasticity Redox Dimerization |
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