Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast

Takizawa, Peter A.; Sil, Anita; Swedlow, Jason R.; Herskowitz, Ira; Vale, Ronald D.

doi:10.1038/38015

Cited by 358 publications

(347 citation statements)

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“…This provides an explanation for the inability of bni1⌬ yeast to undergo tip-directed growth (Evangelista et al, 1997;Mosch and Fink, 1997;Sheu et al, 2000;OzakiKuroda et al, 2001) or to bud in a bipolar manner (Zahner et al, 1996), which in turn requires tip-directed growth (Sheu et al, 2000). Other myosin-V-dependent cargoes also lose their tip-association in bni1⌬ cells, including the microtubule anchoring protein Kar9p (Miller et al, 1999), cytoplasmic microtubules (Segal et al, 2000), and the ASH1 mRNA (Takizawa et al, 1997;Beach et al, 1999), explaining the inability of bni1⌬ yeast to orient the mitotic spindle early in the cell cycle Lee et al, 1999) or to properly restrict Ash1p-mediated cell differentiation to daughter cells (Jansen et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

Pruyne

Gao

et al. 2004

MBoC

151

208

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Bud growth in yeast is guided by myosin-driven delivery of secretory vesicles from the mother cell to the bud. We find transport occurs along two sets of actin cables assembled by two formin isoforms. The Bnr1p formin assembles cables that radiate from the bud neck into the mother, providing a stable mother-bud axis. These cables also depend on septins at the neck and are required for efficient transport from the mother to the bud. The Bni1p formin assembles cables that line the bud cortex and target vesicles to varying locations in the bud. Loss of these cables results in morphological defects as vesicles accumulate at the neck. Assembly of these cables depends on continued polarized secretion, suggesting vesicular transport provides a positive feedback signal for Bni1p activation, possibly by rho-proteins. By coupling different formin isoforms to unique cortical landmarks, yeast uses common cytoskeletal elements to maintain stable and dynamic axes in the same cell. INTRODUCTIONProper cell polarization requires a balance between dynamism and stability. Persistent systems, such as the apical and basolateral domains of epithelial cells, show a higher stability than flexible systems, such as cells undergoing chemotaxis. However, both types can use similar cytoskeletal components, so an important task in understanding the control of polarity is to identify features that influence persistence, and how those features integrate with the core cytoskeletal machinery providing the physical expression of polarity.The process of bud growth of the yeast Saccharomyces cerevisiae provides a model for examining the control of polarity (for reviews, see Bretscher, 2003;Chang and Peter, 2003). Secretory organelles, such as the Golgi and endoplasmic reticulum, are distributed throughout the bud and mother cell, whereas post-Golgi secretory vesicles concentrate at discrete growth sites at the cell cortex. These vesicles are guided to these sites along what are essentially two axes of polarity: a stable axis directing traffic from the mother into the bud, and a dynamic axis that fine-tunes delivery from the bud neck to specific regions in the bud, sending vesicles first to the small bud tip, then to the entire bud surface, and finally back toward the neck during mother/daughter separation. On delivery to these locations, post-Golgi vesicles fuse with the cell surface to promote localized cell expansion.Two class-V myosins, with heavy chains encoded by MYO2 (Johnston et al., 1991) and MYO4 (Haarer et al., 1994), propel cellular components, including vesicles, organelles, mRNAs, and microtubules, from the mother into the bud during growth and organelle segregation. The myosins move along cables of actin filaments that radiate throughout the cell in arrays oriented toward growth sites (Adams and Pringle, 1984;Kilmartin and Adams, 1984).Assembly of these cables depends on two formin homologues, Bni1p and Bnr1p (Evangelista et al., 2002;Sagot et al., 2002a), members of a family of cytoskeletal regulatory proteins defined by conserved fo...

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Section: Discussionmentioning

confidence: 99%

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

Pruyne

Gao

et al. 2004

MBoC

151

208

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“…The lovely details of HO regulation ± which involve such gems as a transcriptional repressor migrating along cytoskeletal ®bers to selectively invade one of two nuclei in a mother-daughter pair! (Bobola et al, 1996;Sil and Herskowitz, 1996;Takizawa et al, 1997) ± are outside the scope of this review. For present purposes, two things are important: (i) activation of the gene requires both SWI/SNF (Stern et al, 1984) and the HAT Gcn5p (Pollard and ; (ii) HO upregulation occurs at a very de®ned timepoint in the cell cycle ± ca.…”

Section: Ho Endonuclease Gene Activation: Mating As Serious Businessmentioning

confidence: 98%

Chromatin remodeling and transcriptional activation: the cast (in order of appearance)

2001

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The number of chromatin modifying and remodeling complexes implicated in genome control is growing faster than our understanding of the functional roles they play. We discuss recent in vitro experiments with biochemically de®ned chromatin templates that illuminate new aspects of action by histone acetyltransferases and ATPdependent chromatin remodeling engines in facilitating transcription. We review a number of studies that present an`ordered recruitment' view of transcriptional activation, according to which various complexes enter and exit their target promoter in a set sequence, and at speci®c times, such that action by one complex sets the stage for the arrival of the next one. A consensus emerging from all these experiments is that the joint action by several types of chromatin remodeling machines can lead to a more profound alteration of the infrastructure of chromatin over a target promoter than could be obtained by these enzymes acting independently. In addition, it appears that in speci®c cases one type of chromatin structure alteration (e.g., histone hyperacetylation) is contingent upon prior alterations of a di erent sort (i.e., ATP-dependent remodeling of histone-DNA contacts). The striking di erences between the precise sequence of action by various cofactors observed in these studies may be ± at least in part ± due to di erences between the speci®c promoters studied, and distinct requirements exhibited by speci®c loci for chromatin remodeling based on their pre-existing nucleoprotein architecture. Oncogene (2001) 20, 2991 ± 3006.

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“…With more than 30 mRNAs localized at the bud tip, the budding yeast Saccharomyces cerevisiae is an excellent model system for studying the mechanisms behind mRNA transport and localization Darzacq et al, 2003). One of these transcripts is the ASH1 mRNA, which is localized at the distal tip of daughter cells during late anaphase (Long et al, 1997;Takizawa et al, 1997). This localization promotes the asymmetric sorting of Ash1p to the daughter cell nucleus and results in the inhibition of mating-type switching in the daughter cell (Jansen et al, 1996;Sil and Herskowitz, 1996).…”

Section: Introductionmentioning

confidence: 99%

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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Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast

Cited by 358 publications

References 1 publication

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

Stable and Dynamic Axes of Polarity Use Distinct Formin Isoforms in Budding Yeast

Chromatin remodeling and transcriptional activation: the cast (in order of appearance)

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

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