A Novel Transport Pathway for a Yeast Plasma Membrane Protein Encoded by a Localized mRNA

Jüschke, Christoph; Ferring, Dunja; Jansen, Ralf‐Peter; Seedorf, Matthias

doi:10.1016/j.cub.2004.02.034

Cited by 53 publications

(72 citation statements)

References 16 publications

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“…IST2 mRNA, which is also translocated by Myo4p, contains only one localization element (25). Consistent with our interpretation, IST2 mRNA is less efficiently transported and is less stringently localized to the bud tip (36).…”

Section: Discussionsupporting

confidence: 90%

Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes

Heuck

Jellbauer

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Myosin-motors are conserved from yeast to human and transport a great variety of cargoes. Most plus-end directed myosins, which constitute the vast majority of all myosin motors, form stable dimers and interact constitutively with their cargo complexes. To date, little is known about regulatory mechanisms for cargocomplex assembly. In this study, we show that the type V myosin Myo4p binds to its cargo via two distinct binding regions, the C-terminal tail and a coiled-coil domain-containing fragment. Furthermore, we find that Myo4p is strictly monomeric at physiologic concentrations. Because type V myosins are thought to require dimerization for processive movement, a mechanism must be in place to ensure that oligomeric Myo4p is incorporated into cargotranslocation complexes. Indeed, we find that artificial dimerization of the Myo4p C-terminal tail promotes stabilization of myosincargo complexes, suggesting that full-length Myo4p dimerizes in the cocomplex as well. We also combined the Myo4p C-terminal tail with the coiled-coil region, lever arm, and motor domain from a different myosin to form constitutively dimeric motor proteins. This heterologous motor successfully translocates its cargo in vivo, suggesting that wild-type Myo4p may also function as a dimer during cargo-complex transport.cell asymmetry ͉ Myo4p ͉ RNA localization ͉ She3p ͉ motor protein

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Section: Discussionsupporting

confidence: 90%

Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes

Heuck

Jellbauer

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…In addition to its role in oocytes, Trailer hitch is likely to be involved in RNA localization in other cells types and for general cellular functions such as ER exit-site formation, which is postulated to involve RNA localization (14,44,45). The mouse genome contains a single trailer hitch gene, but its function has not yet been characterized (46).…”

Section: Resultsmentioning

confidence: 99%

Mouse oocytes within germ cell cysts and primordial follicles contain a Balbiani body

Pepling

Wilhelm

O'Hara

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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184

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The Balbiani body or mitochondrial cloud is a large distinctive organelle aggregate found in developing oocytes of many species, but its presence in the mouse has been controversial. Using confocal and electron microscopy, we report that a Balbiani body does arise in mouse neonatal germline cysts and oocytes of primordial follicles but disperses as follicles begin to grow. The mouse Balbiani body contains a core of Golgi elements surrounded by mitochondria and associated endoplasmic reticulum. Because of their stage specificity and perinuclear rather than spherical distribution, these clustered Balbiani body mitochondria may have been missed previously. The Balbiani body also contains Trailer hitch, a widely conserved member of a protein complex that associates with endoplasmic reticulum/Golgi-like vesicles and transports specific RNAs during Drosophila oogenesis. Our results provide evidence that mouse oocytes develop using molecular and developmental mechanisms widely conserved throughout the animal kingdom.germ plasm ͉ gamete biology ͉ oocyte development ͉ ovary ͉ oogenesis

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“…Membrane fractionation was performed as previously described (Juschke et al, 2004). Briefly, logarithmically growing cells were washed in 20 mM HEPES, pH 7.5, 20 mM NaF, and 20 mM NaN 3 .…”

Section: Subcellular Fractionationmentioning

confidence: 99%

α-Synuclein–induced Aggregation of Cytoplasmic Vesicles inSaccharomyces cerevisiae

Soper¹,

Roy²,

Stieber³

et al. 2008

MBoC

147

168

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Aggregated ␣-synuclein (␣-syn) fibrils form Lewy bodies (LBs), the signature lesions of Parkinson's disease (PD) and related synucleinopathies, but the pathogenesis and neurodegenerative effects of LBs remain enigmatic. Recent studies have shown that when overexpressed in Saccharomyces cerevisiae, ␣-syn localizes to plasma membranes and forms cytoplasmic accumulations similar to human ␣-syn inclusions. However, the exact nature, composition, temporal evolution, and underlying mechanisms of yeast ␣-syn accumulations and their relevance to human synucleinopathies are unknown. Here we provide ultrastructural evidence that ␣-syn accumulations are not comprised of LB-like fibrils, but are associated with clusters of vesicles. Live-cell imaging showed ␣-syn initially localized to the plasma membrane and subsequently formed accumulations in association with vesicles. Imaging of truncated and mutant forms of ␣-syn revealed the molecular determinants and vesicular trafficking pathways underlying this pathological process. Because vesicular clustering is also found in LB-containing neurons of PD brains, ␣-syn-mediated vesicular accumulation in yeast represents a model system to study specific aspects of neurodegeneration in PD and related synucleinopathies. INTRODUCTIONParkinson's disease (PD) is the most prevalent neurodegenerative movement disorder and is characterized by bradykinesia, rigidity, postural instability, and resting tremor (Galvin et al., 2001;Forman et al., 2005), as well as by the loss of dopaminergic neurons and presence of neuronal inclusions, known as Lewy bodies (LBs) and Lewy neurites (Forman et al., 2005). The identification of an ␣-syn gene (SNCA) mutation associated with autosomal dominant PD (Polymeropoulos et al., 1997), and the identification of fibrillar ␣-syn as the principal component of LB pathology (Spillantini et al., 1997), indicate that the LBs formed by ␣-syn define classic PD and are implicated in disease pathogenesis. The subsequent identification of additional disease-linked SNCA mutations (Polymeropoulos et al., 1997;Kruger et al., 1998;Zarranz et al., 2004), as well as replications of the SNCA gene (Singleton et al., 2003;Chartier-Harlin et al., 2004), indicate that both mutant ␣-syn and increased expression of wildtype (WT) ␣-syn can cause neurodegeneration.In addition to PD, filamentous ␣-syn inclusions have been detected in other neurodegenerative diseases including the LB variant of Alzheimer's disease, dementia with LBs, neurodegeneration with brain iron accumulation type-1, and multiple system atrophy, which are collectively known as synucleinopathies (Spillantini et al., 1997;Duda et al., 2000). ␣-syn fibrils exhibit properties of amyloid (Spillantini et al., 1998), and ␣-syn assembles into amyloid fibrils in vitro (Han et al., 1995;Giasson et al., 1999), whereas SNCA mutations can accelerate ␣-syn fibrillization (Conway et al., 1998;Greenbaum et al., 2005). Therefore, it is plausible that ␣-syn misfolds and aggregates into amyloid fibrils that are neurotoxic and play a cau...

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A Novel Transport Pathway for a Yeast Plasma Membrane Protein Encoded by a Localized mRNA

Cited by 53 publications

References 16 publications

Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes

Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes

Mouse oocytes within germ cell cysts and primordial follicles contain a Balbiani body

α-Synuclein–induced Aggregation of Cytoplasmic Vesicles inSaccharomyces cerevisiae

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