Two single-headed myosin V motors bound to a tetrameric adapter protein form a processive complex

Krementsova, Elena B.; Hodges, Alex R.; Bookwalter, Carol S.; Sladewski, Thomas E.; Travaglia, Mirko; Sweeney, H. Lee; Trybus, Kathleen M.

doi:10.1083/jcb.201106146

Cited by 31 publications

(55 citation statements)

References 55 publications

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“…Contrary to the proposal (13,16,26) that Myo4p•She3p form a 1:1 heterodimer, our data show that Myo4p and She3p associate instead in a 1:2 heterotrimer. Specifically, we found that a pseudocoiled-coil region of two She3p molecules forms an extensive binding platform for the C-terminal domain (CTD) of a single Myo4p molecule.…”

Section: Significancecontrasting

confidence: 55%

“…1B and 5A). Collectively, these data overturn the view that Myo4p and She3p associate with each other as a 1:1 heterodimer and are doing so via a dedicated helical region in each molecule (13,23,26). They also contradict the idea that Myo4p and She3p molecules can associate with each other to form a complex of two Myo4p molecules and an unspecified number of She3p molecules (25).…”

Section: Discussioncontrasting

confidence: 43%

“…To obtain a transport-competent motor complex with two Myo4p molecules, two such Myo4p•She3p heterodimers had to be linked together. Initially, it was reported that only She2p tetramer, i.e., without added zipcode RNA, was sufficient to carry out coupling of two Myo4p•She3p heterodimers and thereby to generate a motor complex with the obligatory two Myo4p molecules (13). However, in an in vitro reconstitution experiment (concurrent to our work) carried out at physiological salt concentration, both She2p and zipcoded mRNA were reported to be required for the assembly of a transport-competent motor complex.…”

Section: Significancementioning

confidence: 42%

“…In this model, neither zipcode RNA nor She2p was directly involved in generating a cytoplasmic Myo4p•She3p complex containing two myosin molecules. Another model proposed that a dedicated helical region downstream from the lever arm of Myo4p interacts with a helical region of She3p to form a heterocoiled coil, i.e., a 1:1 Myo4p•She3p heterodimer (13,16,26). To obtain a transport-competent motor complex with two Myo4p molecules, two such Myo4p•She3p heterodimers had to be linked together.…”

Section: Significancementioning

confidence: 99%

“…The components of the motor complex for the zipcoded mRNA transport system in yeast were identified some time ago (11): (i) Myosin 4 protein (Myo4p) (also known as She1p), one of five distinct myosin heavy chains in yeast (each Myo4p "lever arm" portion is predicted to be associated with five identical light chains); (ii) She2p, a tetramer that specifically binds to mRNA zipcode (12)(13)(14)(15); and (iii) swi5p-dependent HO expression 3 protein (She3p), a multimodule "adaptor" protein that serves as linker between She2p and the C-terminal domain (CTD) of Myo4p (16,17). She4p is another member of the "She family"; it forms a homodimer that interacts with the motor domain of Myo4p (18).…”

mentioning

confidence: 99%

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Structure of a myosin•adaptor complex and pairing by cargo

Shi

Singh

Esselborn

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Significance To navigate large cargo through the viscous cytoplasm, cells use a variety of energy-consuming machines that, akin to ropewalkers, move on intracellular “tracks” in a stepwise “bipedal” fashion. To prevent waste of energy by futile walking, several control mechanisms have evolved. In the case described here for one group of yeast myosins, crystallographic and biophysical analyses revealed that a single myosin molecule associates with an intertwined middle region of two “adaptor” molecules. The adaptor also contains distinct binding sites for cargo. Only when cargo is attached to the myosin-bound adaptor are two of the myosin–adaptor complexes joined into a pair, akin to converting a uniped (unable to walk) into a biped (able to walk).

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Section: Significancecontrasting

confidence: 55%

Section: Discussioncontrasting

confidence: 43%

Section: Significancementioning

confidence: 42%

Section: Significancementioning

confidence: 99%

mentioning

confidence: 99%

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Structure of a myosin•adaptor complex and pairing by cargo

Shi

Singh

Esselborn

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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mRNA transport in fungal top models

et al. 2017

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Eukaryotic cells rely on the precise determination of when and where proteins are synthesized. Spatiotemporal expression is supported by localization of mRNAs to specific subcellular sites and their subsequent local translation. This holds true for somatic cells as well as for oocytes and embryos. Most commonly, mRNA localization is achieved by active transport of the molecules along the actin or microtubule cytoskeleton. Key factors are molecular motors, adaptors, and RNA-binding proteins that recognize defined sequences or structures in cargo mRNAs. A deep understanding of this process has been gained from research on fungal model systems such as Saccharomyces cerevisiae and Ustilago maydis. Recent highlights of these studies are the following: (1) synergistic binding of two RNA-binding proteins is needed for high affinity recognition; (2) RNA sequences undergo profound structural rearrangements upon recognition; (3) mRNA transport is tightly linked to membrane trafficking; (4) mRNAs and ribosomes are transported on the cytoplasmic surface of endosomes; and (5) heteromeric protein complexes are, most likely, assembled co-translationally during endosomal transport. Thus, the study of simple fungal model organisms provides valuable insights into fundamental mechanisms of mRNA transport boosting the understanding of similar events in higher eukaryotes.

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The Functions and Regulatory Principles of mRNA Intracellular Trafficking

Bergalet

Lécuyer

2014

Systems Biology of RNA Binding Proteins

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The subcellular localization of RNA molecules is a key step in the control of gene expression that impacts a broad array of biological processes in different organisms and cell types. Like other aspects of posttranscriptional gene regulation discussed in this collection of reviews, the intracellular trafficking of mRNAs is modulated by a complex regulatory code implicating specific cis-regulatory elements, RNA-binding proteins, and cofactors that function combinatorially to dictate precise localization mechanisms. In this review, we first discuss the functional benefits of transcript localization, the regulatory principles involved, and specific molecular mechanisms that have been described for a few well-characterized mRNAs. We also overview some of the emerging genomic and imaging technologies that have provided significant insights into this layer of gene regulation. Finally, we highlight examples of human diseases where defective transcript localization has been documented.

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Two single-headed myosin V motors bound to a tetrameric adapter protein form a processive complex

Abstract: The yeast class V myosin Myo4p moves processively in vivo in a cargo-dependent manner following formation of a double-headed complex with the adapter protein She3p and the mRNA-binding protein She2p.

Cited by 31 publications

References 55 publications

Structure of a myosin•adaptor complex and pairing by cargo

Structure of a myosin•adaptor complex and pairing by cargo

mRNA transport in fungal top models

The Functions and Regulatory Principles of mRNA Intracellular Trafficking

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