Identification of an organelle-specific myosin V receptor

Ishikawa, Kuniko; Catlett, Natalie L.; Novák, J; Tang, Fusheng; Nau, Johnathan J.; Weisman, Lois S.

doi:10.1083/jcb.200210139

Cited by 107 publications

(132 citation statements)

References 30 publications

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“…For each of its functions, Vac8 interacts with specific proteins (Pan and Goldfarb, 1998;Wang et al, 1998;Scott et al, 2000;Veit et al, 2001;Ishikawa et al, 2003). Therefore, palmitoylation of Vac8 could directly affect these interactions, either by forming direct lipid-protein interactions or by inducing conformational changes that permit certain protein-protein interactions.…”

Section: Discussionmentioning

confidence: 99%

Palmitoylation determines the function of Vac8 at the yeast vacuole

Subramanian

Dietrich

Hou

et al. 2006

Journal of Cell Science

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Palmitoylation stably anchors specific proteins to membranes, but may also have a direct effect on the function of a protein. The yeast protein Vac8 is required for efficient vacuole fusion, inheritance and cytosol-to-vacuole trafficking. It is anchored to vacuoles by an N-terminal myristoylation site and three palmitoylation sites, also known as the SH4 domain. Here, we address the role of Vac8 palmitoylation and show that the position and number of substrate cysteines within the SH4 domain determine the vacuole localization of Vac8: stable vacuole binding of Vac8 requires two cysteines within the N-terminus, regardless of the combination. Importantly, our data suggest that palmitoylation adds functionality to Vac8 beyond simple localization. A mutant Vac8 protein, in which the palmitoylation sites were replaced by a stretch of basic residues, still localizes to vacuole membranes and functions in cytosol-to-vacuole transport, but can only complement the function of Vac8 in morphology and inheritance if it also contains a single cysteine within the SH4 domain. Our data suggest that palmitoylation is not a mere hydrophobic anchor required solely for localization, but influences the protein function(s).

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Section: Discussionmentioning

confidence: 99%

Palmitoylation determines the function of Vac8 at the yeast vacuole

Subramanian

Dietrich

Hou

et al. 2006

Journal of Cell Science

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“…74 For inheritance, it binds via the adaptor protein Vac17 and the myosin Myo2 to actin. 204,205 It also interacts with the ER protein Nvj1 to establish contact zones between the ER and vacuole, 206 and it is part of a complex of phosphoproteins involved in the Cvt pathway and autophagy. 21 On isolated vacuoles, Vac8 becomes palmitoylated prior to the ATP-dependent priming reaction.…”

Section: Protein Palmitoylation and Vacuole Fusionmentioning

confidence: 99%

Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics

Ostrowicz¹,

Meiringer²,

Ungermann³

2008

Autophagy

102

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Vesicular transport in eukaryotic cells is concluded with the consumption of the vesicle at the target membrane. This fusion process relies on Rabs, tethers and SNAREs. Powerful in vitro fusion systems using isolated organelles were crucial to obtain insights into the underlying mechanism of membrane fusionfrom the initiation of fusion to lipid bilayer mixing. Among these systems, yeast vacuoles turned out to be particularly useful as they can be manipulated biochemically and genetically. Studies relying on this organelle have revealed insights into the connection of vacuole fusion to endomembrane biogenesis. A number of fusion factors were identified and characterized over the last several years, and placed into the fusion cascade. Within this review, we will present and discuss the current state of our knowledge on vacuole fusion.

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“…Vacuoles were labeled in vivo with N-(3-triethelammoniumpropyl)-4-(6 (4-(diethylamino) phenyl) hexatrienyl) pyridinium dibromide (FM4-64; Molecular Probes, Eugene, OR) essentially as described (Ishikawa et al, 2003). In brief, a 2 mg/ml stock solution of FM4-64 in DMSO was added to early log phase cultures for a final concentration of 80 M. After 1 h of labeling, cells were washed and were then chased in fresh liquid medium for 3-4 h.…”

Section: In Vivo Labeling Of Vacuolesmentioning

confidence: 99%

“…For example, vacuole inheritance utilizes the actin cytoskeleton and the class-V myosin complex, composed of Myo2p, Vac17p, and Vac8p (Hill et al, 1996;Wang et al, 1998;Ishikawa et al, 2003;Tang et al, 2003). Myo2p is one of two class-V myosin motors in budding yeast.…”

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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Identification of an organelle-specific myosin V receptor

Cited by 107 publications

References 30 publications

Palmitoylation determines the function of Vac8 at the yeast vacuole

Palmitoylation determines the function of Vac8 at the yeast vacuole

Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics

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

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