Association of the Yeast RNA-binding Protein She2p with the Tubular Endoplasmic Reticulum Depends on Membrane Curvature

Genz, Christian; Fundakowski, Julia; Hermesh, Orit; Schmid, Maria; Jansen, Ralf‐Peter

doi:10.1074/jbc.m113.486431

Cited by 30 publications

(39 citation statements)

References 55 publications

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“…Similar observations have been made for genes that are essential for the early steps of ER inheritance, for cER docking at the bud tip (Aronov et al, 2007;Fundakowski et al, 2012) or for the formation of ER tubules (Fundakowski et al, 2012). Furthermore, the RNA-binding protein She2p co-fractionates with ER membranes and can bind to protein-free liposomes with a membrane curvature similar to that of ER tubules, suggesting that this protein connects localized mRNAs to ER (Genz et al, 2013). These findings led to the idea that localized mRNAs encoding membrane or ER proteins travel to the bud by associating with cER tubules.…”

Section: Introductionsupporting

confidence: 49%

“…The stronger binding of She2p to liposomes with an increasing PtdEtn content supports a more specific role of PtdEtn. Previous experiments have not indicated a role for specific lipids in She2p binding (Genz et al, 2013); however, this conclusion was based on the fact that the omission of phospholipids with negative net charge, like PtdSer and phosphatidylinositol, did not alter She2p binding. However, PtdEtn was not tested in this system.…”

Section: Discussionmentioning

confidence: 62%

“…We have previously shown that the mRNA localization factor She2p can directly bind to protein-free liposomes (Genz et al, 2013). In order to test whether PtdEtn influences She2p binding, we generated 80-nm diameter liposomes with increasing PtdEtn contents ranging from 0% to 50% (see Materials and Methods), incubated them with recombinant She2p and performed a flotation analysis to determine the amount of She2p that fractionated with (and thus bound to) liposomes (Genz et al, 2013).…”

Section: She2p Binding To Membranes Increases With Ptdetn Levelsmentioning

confidence: 99%

“…3A, bottom row). The RNA-binding protein She2p can associate with membranes in vitro and co-purifies with ER from cell extracts (Aronov et al, 2007;Genz et al, 2013;Schmid et al, 2006). In order to test whether the ER-localized WSC2-MS2L mRNPs in the mother cell are still associated with She2p, we co-expressed a GFP-tagged She2p with WSC2-MS2L and detected the mRNA by means of a fusion of the MS2 coat protein to five mCherry molecules (see Materials and Methods).…”

Section: Association Of Mislocalized Mrnps With Aberrant Er Structurementioning

confidence: 99%

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Yeast phospholipid biosynthesis is linked to mRNA localization

Hermesh

Genz

Yofe

et al. 2014

Journal of Cell Science

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Regulation of the localization of mRNAs and local translation are universal features in eukaryotes and contribute to cellular asymmetry and differentiation. In Saccharomyces cerevisiae, localization of mRNAs that encode membrane proteins requires the She protein machinery, including the RNA-binding protein She2p, as well as movement of the cortical endoplasmic reticulum (cER) to the yeast bud. In a screen for ER-specific proteins necessary for the directional transport of WSC2 and EAR1 mRNAs, we have identified enzymes that are involved in phospholipid metabolism. Loss of the phospholipid methyltransferase Cho2p, which showed the strongest impact on mRNA localization, disturbs mRNA localization, as well as ER morphology and segregation, owing to an increase in the amount of cellular phosphatidylethanolamine (PtdEtn). Mislocalized mRNPs containing She2p colocalize with aggregated cER structures, suggestive of the entrapment of mRNA and She2p by the elevated PtdEtn level. This was confirmed by the elevated binding of She2p to PtdEtn-containing liposomes. These findings underscore the importance of ER membrane integrity in mRNA transport.

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Section: Introductionsupporting

confidence: 49%

Section: Discussionmentioning

confidence: 62%

Section: She2p Binding To Membranes Increases With Ptdetn Levelsmentioning

confidence: 99%

Section: Association Of Mislocalized Mrnps With Aberrant Er Structurementioning

confidence: 99%

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Yeast phospholipid biosynthesis is linked to mRNA localization

Hermesh

Genz

Yofe

et al. 2014

Journal of Cell Science

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“…She3p contains at least three binding modules, one for Myo4p and two for cargos, as diverse as zipcoded mRNP and tubular endoplasmic reticulum (tER) (27)(28)(29). She3p's binding site for Myo4p has been localized to the middle region of She3p (30), with a genetically determined upstream binding site for tER and a downstream binding site for zipcoded mRNP (29).…”

Section: Significancementioning

confidence: 99%

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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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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Association of the Yeast RNA-binding Protein She2p with the Tubular Endoplasmic Reticulum Depends on Membrane Curvature

Cited by 30 publications

References 55 publications

Yeast phospholipid biosynthesis is linked to mRNA localization

Yeast phospholipid biosynthesis is linked to mRNA localization

Structure of a myosin•adaptor complex and pairing by cargo

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

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