A Role for Actin, Cdc1p, and Myo2p in the Inheritance of Late Golgi Elements in<i>Saccharomyces cerevisiae</i>

Rossanese, Olivia W.; Reinke, Catherine; Bevis, Brooke J.; Hammond, Adam T.; Sears, Irina B.; O’Connor, J. P.; Glick, Benjamin S.

doi:10.1083/jcb.153.1.47

Cited by 196 publications

(195 citation statements)

References 86 publications

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“…Therefore, it might be the defect of actin cable-based transport, which leads to the phenotype observed when AgBNI1 is deleted. It is known from several studies, that actin cables can serve as tracks for different cargos such as secretory vesicles (Johnston et al, 1991) and several organelles (Simon et al, 1995;Hill et al, 1996;Hoepfner et al, 2001;Rossanese et al, 2001) as well as mRNA (Bobola et al, 1996;Sil and Herskowitz, 1996;Takizawa et al, 2000). Using the AgSec4p fused to GFP, we were able to show that secretory vesicles use actin cables for accumulation at the hyphal tips.…”

Section: Agbni1p and The Actin Cytoskeletonmentioning

confidence: 58%

From Function to Shape: A Novel Role of a Formin in Morphogenesis of the FungusAshbya gossypii

Schmitz

Kaufmann

Köhli

et al. 2006

MBoC

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Morphogenesis of filamentous ascomycetes includes continuously elongating hyphae, frequently emerging lateral branches, and, under certain circumstances, symmetrically dividing hyphal tips. We identified the formin AgBni1p of the model fungus Ashbya gossypii as an essential factor in these processes. AgBni1p is an essential protein apparently lacking functional overlaps with the two additional A. gossypii formins that are nonessential. Agbni1 null mutants fail to develop hyphae and instead expand to potato-shaped giant cells, which lack actin cables and thus tip-directed transport of secretory vesicles. Consistent with the essential role in hyphal development, AgBni1p locates to tips, but not to septa. The presence of a diaphanous autoregulatory domain (DAD) indicates that the activation of AgBni1p depends on Rho-type GTPases. Deletion of this domain, which should render AgBni1p constitutively active, completely changes the branching pattern of young hyphae. New axes of polarity are no longer established subapically (lateral branching) but by symmetric divisions of hyphal tips (tip splitting). In wild-type hyphae, tip splitting is induced much later and only at much higher elongation speed. When GTP-locked Rho-type GTPases were tested, only the young hyphae with mutated AgCdc42p split at their tips, similar to the DAD deletion mutant. Two-hybrid experiments confirmed that AgBni1p interacts with GTP-bound AgCdc42p. These data suggest a pathway for transforming one axis into two new axes of polar growth, in which an increased activation of AgBni1p by a pulse of activated AgCdc42p stimulates additional actin cable formation and tip-directed vesicle transport, thus enlarging and ultimately splitting the polarity site.

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Section: Agbni1p and The Actin Cytoskeletonmentioning

confidence: 58%

From Function to Shape: A Novel Role of a Formin in Morphogenesis of the FungusAshbya gossypii

Schmitz

Kaufmann

Köhli

et al. 2006

MBoC

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“…Sec7-GFP structures also decreased in number after shift to the nonpermissive temperature. On the other hand, structures bearing the early Golgi markers Och1p-HA (Harris and Waters, 1996) and Sec21p-GFP (Rossanese et al, 2001) were still present after shift to the nonpermissive temperature (Figure 4). Sec21p-GFP was present in a pattern of spots in all four mutants even after shift to the nonpermissive temperature for 40 min (Figure 4 and our unpublished data).…”

Section: Resultsmentioning

confidence: 99%

“…We carried out live imaging of yeast cells as previously described (Rossanese et al, 2001) with minor modifications. To immobilize cells for imaging, a LabTek chamber slide (Nalge Nunc International, Rochester, NY) was pretreated with 2 mg/ml concanavalin A (Sigma, St. Louis, MO, L-7647), rinsed with distilled water, and dried.…”

Section: Microscopy Of Living Cellsmentioning

confidence: 99%

“…Strain CJY101 gea1⌬ gea2⌬/pCLJ92 was constructed by replacing the GEA2 open reading frame with HIS3 in BY4742 gea1⌬ carrying pCLJ92. SEC21-3xGFP strains CJY102/pSKP60, CJY102/pSKP61, CJY102/pSKP62, CJY102/ pSKP63, and CJY102/pSKP64 were constructed from CJY101/pCLJ92 by plasmid shuffling on 5-FOA and then by pop-in-pop-out replacement of SEC21 with SEC21-3xGFP as described (Rossanese et al, 2001). Briefly, CJY101/pSKP60, CJY101/pSKP61, CJY101/pSKP62, CJY101/pSKP63, and CJY101/pSKP64 cells were transformed with YIplac211-SEC21-3xGFP selecting for "pop-in" integration in medium lacking uracil and then grown on 5-FOA to select for "pop-out" events that reconstitute SEC21-3xGFP at the chromosomal SEC21 locus.…”

Section: Mutagenesis and Construction Of Gea2-ts Strainsmentioning

confidence: 99%

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Mutations in a Highly Conserved Region of the Arf1p ActivatorGEA2Block Anterograde Golgi Transport but Not COPI Recruitment to Membranes

Park

Hartnell

Jackson

2005

MBoC

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We have identified an important functional region of the yeast Arf1 activator Gea2p upstream of the catalytic Sec7 domain and characterized a set of temperature-sensitive (ts) mutants with amino acid substitutions in this region. These gea2-ts mutants block or slow transport of proteins traversing the secretory pathway at exit from the endoplasmic reticulum (ER) and the early Golgi, and accumulate both ER and early Golgi membranes. No defects in two types of retrograde trafficking/sorting assays were observed. We find that a substantial amount of COPI is associated with Golgi membranes in the gea2-ts mutants, even after prolonged incubation at the nonpermissive temperature. COPI in these mutants is released from Golgi membranes by brefeldin A, a drug that binds directly to Gea2p and blocks Arf1 activation. Our results demonstrate that COPI function in sorting of at least three retrograde cargo proteins within the Golgi is not perturbed in these mutants, but that forward transport is severely inhibited. Hence this region of Gea2p upstream of the Sec7 domain plays a role in anterograde transport that is independent of its role in recruiting COPI for retrograde transport, at least of a subset of Golgi-ER cargo.

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“…Late-Golgi elements are moved by Myo2p with Ypt11p, a Rab GTPase, and Ret2p, a subunit of the coatomer complex (Rossanese et al, 2001;Arai et al, 2008). Secretory vesicles are moved by Myo2p (Pruyne et al, 1998;Schott et al, 1999) and require the Rab GTPases Ypt31p and Ypt32p (Casavola et al, 2008;Lipatova et al, 2008).…”

Section: Introductionmentioning

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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A Role for Actin, Cdc1p, and Myo2p in the Inheritance of Late Golgi Elements inSaccharomyces cerevisiae

Cited by 196 publications

References 86 publications

From Function to Shape: A Novel Role of a Formin in Morphogenesis of the FungusAshbya gossypii

From Function to Shape: A Novel Role of a Formin in Morphogenesis of the FungusAshbya gossypii

Mutations in a Highly Conserved Region of the Arf1p ActivatorGEA2Block Anterograde Golgi Transport but Not COPI Recruitment to Membranes

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

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