She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p

Böhl, Florian; Kruse, Claudia; Frank, Andrea; Ferring, Dunja; Jansen, Ralf‐Peter

doi:10.1093/emboj/19.20.5514

Cited by 187 publications

(263 citation statements)

References 46 publications

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“…ASH1 mRNA is transported as an mRNP, consisting of ASH1 mRNA, She2p, She3p, and Myo4p/She1p and other proteins to the distal tip of the bud, where the Ash1 protein is translated and targeted to the daughtercell nucleus (Bertrand et al 1998;Bohl et al 2000;Takizawa and Vale 2000;Irie et al 2002). In this study, we used the TAP method to identify additional protein components associated with this ASH1 mRNP.…”

Section: Discussionmentioning

confidence: 99%

“…The proper delivery of ASH1 mRNA to the bud tip requires a transport particle (the "locasome") containing She2p binding to the four zipcodes as well as to She3p, and assembly of the myosin motor, She1p/Myo4 (Bertrand et al 1998;Bohl et al 2000;Long et al 2000;Takizawa and Vale 2000). However, to effect asymmetry, RNA translation must be temporally repressed before it anchors at the bud tip.…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies have shown that She2p, a 26-kDa RNAbinding protein, is a core component of ASH1 mRNP and plays a key role in the localization process (Bertrand et al 1998;Bohl et al 2000;Long et al 2000). To characterize additional regulatory proteins associated with ASH1 mRNA, we inserted a TAP tag in-frame at the 3Ј end of the SHE2 gene (Puig et al 2001) and purified the ASH1 mRNP with IgG-coated Sepharose.…”

Section: Puf6p Is a Structural Component Of Ash1 Mrnpmentioning

confidence: 99%

“…This specific inheritance of Ash1p results from localizing the ASH1 mRNA to the distal bud tip during anaphase of the cell cycle, where it is presumably translated near the bud nucleus (Long et al 1997;Takizawa et al 1997). The major components required for ASH1 mRNA localization have been identified and were shown to form a large ribonucleoprotein particle ("locasome" or mRNP) containing She1p/Myo4p, a type V myosin that transports ASH1 mRNA in the cytoplasm along cytoskeletal filaments to its final destination (Bertrand et al 1998;Beach et al 1999), She2p, identified as an RNA-binding protein that specifically interacts with the ASH1 mRNA localization zipcodes, and She3p, which serves as a bridge protein between She1p and She2p (Bohl et al 2000;Long et al 2000;Takizawa and Vale 2000).…”

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confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Puf6p Is a Structural Component Of Ash1 Mrnpmentioning

confidence: 99%

mentioning

confidence: 99%

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

et al. 2004

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“…Similarly, the cortical ER is moved by Myo4p, the other yeast myosin-V, which forms a complex with She3p (Estrada et al, 2003). Several mRNAs are also moved by Myo4p and require both She3p and She2p, proteins whose roles are not well established (Bohl et al, 2000;Long et al, 2000;Shepard et al, 2003;Heuck et al, 2007;Hodges et al, 2008). Moreover, rather than attachment to the globular tail, She3p binds the rod of Myo4p.…”

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confidence: 99%

PTC1Is Required for Vacuole Inheritance and Promotes the Association of the Myosin-V Vacuole-specific Receptor Complex

Jin

Eves

Tang

et al. 2009

MBoC

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Organelle inheritance occurs during cell division. In Saccharomyces cerevisiae, inheritance of the vacuole, and the distribution of mitochondria and cortical endoplasmic reticulum are regulated by Ptc1p, a type 2C protein phosphatase. Here we show that PTC1/VAC10 controls the distribution of additional cargoes moved by a myosin-V motor. These include peroxisomes, secretory vesicles, cargoes of Myo2p, and ASH1 mRNA, a cargo of Myo4p. We find that Ptc1p is required for the proper distribution of both Myo2p and Myo4p. Surprisingly, PTC1 is also required to maintain the steady-state levels of organelle-specific receptors, including Vac17p, Inp2p, and Mmr1p, which attach Myo2p to the vacuole, peroxisomes, and mitochondria, respectively. Furthermore, Vac17p fused to the cargo-binding domain of Myo2p suppressed the vacuole inheritance defect in ptc1⌬ cells. These findings suggest that PTC1 promotes the association of myosin-V with its organelle-specific adaptor proteins. Moreover, these observations suggest that despite the existence of organelle-specific receptors, there is a higher order regulation that coordinates the movement of diverse cellular components. INTRODUCTIONDuring each cell cycle, cytoplasmic organelles are actively distributed between dividing cells to maintain organelle copy number and volume. The yeast Saccharomyces cerevisiae is an excellent model system for studying the spatial and temporal control of organelle inheritance. In yeast, several organelles are transmitted from mother to daughter cells. These include the vacuole, mitochondria, the endoplasmic reticulum (ER), late-Golgi elements and peroxisomes (reviewed in Weisman, 2006).Early in the cell cycle, a portion of each organelle is transported into the emerging bud. The polarized transport of most organelles from the mother to the bud is an active process that requires the actin cytoskeleton, myosin-V motors, and receptor proteins, which physically connect the motor to organelle cargoes (Beach et al., 2000;Yin et al., 2000;Boldogh et al., 2001;Barr, 2002;Bretscher, 2003;Du et al., 2004;Fagarasanu et al., 2006bFagarasanu et al., , 2007Weisman, 2006). Thus, formation of a complex between the motor and receptor protein is important for polarized organelle transport.Similar to yeast, in vertebrates, myosin-V motors move cargoes along the actin cytoskeleton. The best studied cargo of vertebrate myosin-V are melanosomes, which are moved in melanocytes by myosin-Va. Melanosomes attach to myosin-Va through Rab27a and melanophilin (Fukuda and Kuroda, 2002;Wu et al., 2002). Rab27a, through geranylgeranylation, attaches to the melanosome membrane, and melanophilin connects myosin-Va and Rab27a. Myosin-V-based intracellular movement has been analyzed in many other eukaryotes, including frogs, fish, mammals, and plants; plant myosin-XI is the functional homologue of yeast and vertebrate myosin-V ( Kinkema and Schiefelbein, 1994;Provance and Mercer, 1999;Tuma and Gelfand, 1999;Desnos et al., 2007;Li and Nebenfuhr, 2007;Sheets et al., 2007;Shimmen, 2007).Ge...

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Signal sequence‐independent targeting of MID2mRNA to the endoplasmic reticulum by the yeast RNA‐binding protein Khd1p

et al. 2018

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Localization of mRNAs depends on specific RNA-binding proteins (RBPs) and critically contributes not only to cell polarization but also to basal cell function. The yeast RBP Khd1p binds to several hundred mRNAs, the majority of which encodes secreted or membrane proteins. We demonstrate that a subfraction of Khd1p associates with artificial liposomes and endoplasmic reticulum (ER), and that Khd1p endomembrane association is partially dependent on its binding to RNA. ER targeting of at least two mRNAs, MID2 and SLG1/WSC1, requires KHD1 but is independent of their translation. Together, our results suggest interdependence of Khd1p and mRNA for their targeting to the ER and presents additional evidence for signal sequence-independent, RBP-mediated mRNA targeting.

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She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p

Cited by 187 publications

References 46 publications

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

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

PTC1Is Required for Vacuole Inheritance and Promotes the Association of the Myosin-V Vacuole-specific Receptor Complex

Signal sequence‐independent targeting of MID2mRNA to the endoplasmic reticulum by the yeast RNA‐binding protein Khd1p

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