ArticleThe Journal of cell biology2010
The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.
Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.The Journal of biological chemistry · 2019Article
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Distinct Roles for the N- and C-terminal Regions of M-Sec in Plasma Membrane Deformation during Tunneling Nanotube Formation.Scientific reports · 2016Article
- Identification of the Isoform-specific Interactions between the Tail and the Head of Class V Myosin.The Journal of biological chemistry · 2016Article
- ASH1 mRNP-core factors form stable complexes in absence of cargo RNA at physiological conditions.RNA biology · 2015Article
- Structural insights into the assembly of a monomeric class V myosin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure of a myosin•adaptor complex and pairing by cargo.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Of social molecules: The interactive assembly of ASH1 mRNA-transport complexes in yeast.RNA biology · 2014Review
- Role of Loc1p in assembly and reorganization of nuclear ASH1 messenger ribonucleoprotein particles in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- In vitro reconstitution of an mRNA-transport complex reveals mechanisms of assembly and motor activation.The Journal of cell biology · 2013Article
- Structural basis of myosin V Rab GTPase-dependent cargo recognition.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural insights into functional overlapping and differentiation among myosin V motors.The Journal of biological chemistry · 2013Article
- Association of the yeast RNA-binding protein She2p with the tubular endoplasmic reticulum depends on membrane curvature.The Journal of biological chemistry · 2013Article
- Purification, crystallization and preliminary crystallographic analysis of the globular domain of the human type V myosin Myo5a.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Whole genome duplication events in plant evolution reconstructed and predicted using myosin motor proteins.BMC evolutionary biology · 2013Article
- Single-molecule reconstitution of mRNA transport by a class V myosin.Nature structural & molecular biology · 2013Article
- Structural basis of cargo recognitions for class V myosins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural insights into the globular tails of the human type v myosins Myo5a, Myo5b, And Myo5c.PloS one · 2013Article
- Principles of mRNA transport in yeast.Cellular and molecular life sciences : CMLS · 2012Review
- Assembly of mRNA-protein complexes for directional mRNA transport in eukaryotes--an overview.Current protein & peptide science · 2012Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Type V myosin (MyoV)-dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2-tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail-lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.