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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structural Insights into Functional Overlapping and Differentiation among Myosin V Motors

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Author(s):
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Nascimento, Andrey F. Z. [1] ; Trindade, Daniel M. [1] ; Tonoli, Celisa C. C. [1] ; de Giuseppe, Priscila O. [1] ; Assis, Leandro H. P. [1] ; Honorato, Rodrigo V. [1] ; de Oliveira, Paulo S. L. [1] ; Mahajan, Pravin [2] ; Burgess-Brown, Nicola A. [2] ; von Delft, Frank [2] ; Larson, Roy E. [3] ; Murakami, Mario T. [1]
Total Authors: 12
Affiliation:
[1] Natl Ctr Res Energy & Mat, Brazilian Biosci Natl Lab, BR-13083970 Campinas, SP - Brazil
[2] Univ Oxford, Struct Genom Consortium, Oxford OX3 7DQ - England
[3] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Cellular & Mol Biol, BR-14049900 Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Journal of Biological Chemistry; v. 288, n. 47, p. 34131-34145, NOV 22 2013.
Web of Science Citations: 16
Abstract

Background: MyoVs are molecular motors widely distributed in eukaryotic cells responsible for membrane trafficking and intracellular transport. Results: The cargo-binding domain from human MyoV paralogs was structurally and biophysically characterized. Conclusion: We identified singular structural changes and molecular events conferring functional differentiation and modulating cargo binding. Significance: This work provides structural insights into cargo recognition and regulatory mechanisms in MyoVs. 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. (AU)

FAPESP's process: 09/08312-6 - Functional and structural investigations of the molecular mechanisms involved in signaling, regulation and activation of Class V myosins
Grantee:Mário Tyago Murakami
Support type: Regular Research Grants