Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p

Kruse, Claudia; Jaedicke, Andreas; Beaudouin, Joël; Böhl, Florian; Ferring, Dunja; Güttler, Thomas; Ellenberg, Jan; Jansen, Ralf‐Peter

doi:10.1083/jcb.200207101

Cited by 63 publications

(110 citation statements)

References 61 publications

(102 reference statements)

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“…This is possibly due to the rapid shutdown of transcription when this strain is shifted at 37°C (Liu et al, 1999). Because She2p nuclear export depends on the nuclear export of newly synthesized mRNAs (Kruse et al, 2002), the shutdown of transcription would explain the absence of nuclear depletion of wild-type She2p in the srp1-31 strain.…”

Section: Discussionmentioning

confidence: 99%

“…Knockouts of these genes disrupt ASH1 mRNA localization and Ash1p sorting to the daughter cell Gu et al, 2004). She2p shuttles between the cytoplasm and the nucleus (Kruse et al, 2002), and recent evidence suggests that the nuclear transit of She2p is involved in the translational regulation of ASH1 mRNA (Du et al, 2008). However, the specific role of She2p in the nucleus is still unclear.…”

Section: Introductionmentioning

confidence: 99%

“…Interacts Directly with the Importin ␣ Srp1p in Order to Enter the Nucleus Previous work has shown that She2p transits through the nucleus (Kruse et al, 2002;Du et al, 2008). Because of its size (26 kDa), which is below the nuclear pore diffusion limit (40 kDa in yeast), a She2p monomer may enter passively through the nuclear pores.…”

Section: Monomeric She2pmentioning

confidence: 99%

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Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

Shen

Paquin

Forget

et al. 2009

MBoC

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The transport and localization of mRNAs results in the asymmetric synthesis of specific proteins. In yeast, the nucleocytoplasmic shuttling protein She2 binds the ASH1 mRNA and targets it for localization at the bud tip by recruiting the She3p-Myo4p complex. Although the cytoplasmic role of She2p in mRNA localization is well characterized, its nuclear function is still unclear. Here, we show that She2p contains a nonclassical nuclear localization signal (NLS) that is essential for its nuclear import via the importin ␣ Srp1p. Exclusion of She2p from the nucleus by mutagenesis of its NLS leads to defective ASH1 mRNA localization and Ash1p sorting. Interestingly, these phenotypes mimic knockouts of LOC1 and PUF6, which encode for nuclear RNA-binding proteins that bind the ASH1 mRNA and control its translation. We find that She2p interacts with both Loc1p and Puf6p and that excluding She2p from the nucleus decreases this interaction. Absence of nuclear She2p disrupts the binding of Loc1p and Puf6p to the ASH1 mRNA, suggesting that nuclear import of She2p is necessary to recruit both factors to the ASH1 transcript. This study reveals that a direct coupling between localization and translation regulation factors in the nucleus is required for proper cytoplasmic localization of mRNAs.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

Shen

Paquin

Forget

et al. 2009

MBoC

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“…Binding of Puf6p to the 3ЈUTR may repress the translation through interaction with translation initiation factors and prevention of ribosome transit. She2p on the zipcodes of the mRNA initiates She3p/Myo4p assembly on the mRNA (Bohl et al 2000;Long et al 2000;Kruse et al 2002) and stabilizes the secondary structure of the zipcodes (Chartrand et al 2002). At the bud tip, Puf6p dissociates from the mRNA as a result of an interaction with an unknown spatially segregated protein, and translation takes place.…”

Section: Discussionmentioning

confidence: 99%

“…The newly transcribed ASH1 mRNA is likely to be associated with Puf6p and other proteins, such as She2p, in the nucleus to form a protein-RNA complex prior to export (Kruse et al 2002). Binding of Puf6p to the 3ЈUTR may repress the translation through interaction with translation initiation factors and prevention of ribosome transit.…”

Section: Discussionmentioning

confidence: 99%

A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization

et al. 2004

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In yeast Saccharomyces cerevisiae, Ash1p, a protein determinant for mating-type switching, is segregated within the daughter cell nucleus to establish asymmetry of HO expression. The accumulation of Ash1p results from ASH1 mRNA that is sorted as a ribonucleoprotein particle (mRNP or locasome) to the distal tip of the bud where translation occurs. To study the mechanism regulating ASH1 mRNA translation, we isolated the ASH1 locasome and characterized the associated proteins by MALDI-TOF. One of these proteins was Puf6p, a new member of the PUF family of highly conserved RNA-binding proteins such as Pumilio in Drosophila, responsible for translational repression, usually to effect asymmetric expression. Puf6p-bound PUF consensus sequences in the 3 UTR of ASH1 mRNA and repressed the translation of ASH1 mRNA both in vivo and in vitro. In the puf6⌬ strain, asymmetric localization of both Ash1p and ASH1 mRNA were significantly reduced. We propose that Puf6p is a protein that functions in the translational control of ASH1 mRNA, and this translational inhibition is necessary before localization can proceed.

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Myosin Va associates with mRNA in ribonucleoprotein particles present in myelinated peripheral axons and in the central nervous system

Calliari

Farías

Puppo

et al. 2014

Developmental Neurobiology

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Sorting of specific mRNAs to particular cellular locations and regulation of their translation is an essential mechanism underlying cell polarization. The transport of RNAs by kinesins and dyneins has been clearly established in several cell models, including neurons in culture. A similar role appears to exist in higher eukaryotes for the myosins. Myosin Va (Myo5a) has been described as a component of ribonucleoprotein particles (RNPs) in the adult rat nervous system and associated to ZBP1 and ribosomes in ribosomal periaxoplasmic plaques (PARPs), making it a likely candidate for mediating some aspects of RNA transport in neurons. To test this hypothesis, we have characterized RNPs containing Myo5a in adult brains of rats and mice. Microarray analysis of RNAs co-immunoprecipitated with Myo5a indicates that this motor may associate with a specific subpopulation of neuronal mRNAs. We found mRNAs encoding α-synuclein and several proteins with functions in translation in these RNPs. Immunofluorescence analyses of RNPs showed apparent co-localization of Myo5a with ribosomes, mRNA and RNA-binding proteins in discrete structures present both in axons of neurons in culture and in myelinated fibers of medullary roots. Our data suggest that PARPs include RNPs bearing the mRNA coding for Myo5a and are equipped with kinesin and Myo5a molecular motors. In conclusion, we suggest that Myo5a is involved in mRNA trafficking both in the central and peripheral nervous systems.

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Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p

Cited by 63 publications

References 61 publications

Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization

Myosin Va associates with mRNA in ribonucleoprotein particles present in myelinated peripheral axons and in the central nervous system

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