The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in <i>Saccharomyces cerevisiae </i>

Altmann, Katrin; Frank, Martina; Neumann, Daniel; Jakobs, Stefan; Westermann, Benedikt

doi:10.1083/jcb.200709099

Cited by 110 publications

(93 citation statements)

References 65 publications

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“…The mitochondrial content in buds is tightly controlled and correlates with the increase of bud size (Rafelski et al, 2012). Anterograde mitochondrial transport along actin cables into the growing bud is mediated by a myosin motor, Myo2 (Altmann et al, 2008;Förtsch et al, 2011). The mitochondrial outer membrane protein Mmr1 anchors mitochondria to bud-tip-localized ER and thereby impedes their transport back into the mother cell (Swayne et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

The yeast cell cortical protein Num1 integrates mitochondrial dynamics into cellular architecture

Klecker

Scholz

Förtsch

et al. 2013

Journal of Cell Science

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101

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SummaryDuring the cell cycle each organelle has to be faithfully partitioned to the daughter cells. However, the mechanisms controlling organellar inheritance remain poorly understood. We studied the contribution of the cell cortex protein, Num1, to mitochondrial partitioning in yeast. Live-cell microscopy revealed that Num1 is required for attachment of mitochondria to the cell cortex and retention in mother cells. Electron tomography of anchoring sites revealed plasma membrane invaginations directly contacting the mitochondrial outer membrane. Expression of chimeric plasma membrane tethers rescued mitochondrial fission defects in Dnum1 and Dmdm36 mutants. These findings provide new insights into the coupling of mitochondrial dynamics, immobilization, and retention during inheritance.

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Section: Introductionmentioning

confidence: 99%

The yeast cell cortical protein Num1 integrates mitochondrial dynamics into cellular architecture

Klecker

Scholz

Förtsch

et al. 2013

Journal of Cell Science

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101

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“…Other yeast organelles are also moved by myosin-V. Mitochondria are moved in part by Myo2p through interaction with Mmr1p and Ypt11p (Itoh et al, 2002(Itoh et al, , 2004Boldogh et al, 2004;Altmann et al, 2008;Valiathan and Weisman, 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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“…The ability of budding yeast myosin-V (Myo2p) to function in organelle and vesicle trafficking relies on its interaction with ELC Mlc1p (Altmann et al, 2008;Wagner et al, 2002). The essential role of the fission yeast ELC (Cdc4p) in contractile ring assembly and cytokinesis (Chang et al, 1996;McCollum et al, 1995) does not depend on myosin-II function because a myosin-II mutant lacking IQ motifs supports normal cytokinesis without suppressing the lethality of cdc4 mutants (D'Souza et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase

Sammons

James

Clayton

et al. 2011

Journal of Cell Science

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SummaryFission yeast myosin-I (Myo1p) not only associates with calmodulin, but also employs a second light chain called Cam2p. cam2 cells exhibit defects in cell polarity and growth consistent with a loss of Myo1p function. Loss of Cam2p leads to a reduction in Myo1p levels at endocytic patches and a 50% drop in the rates of Myo1p-driven actin filament motility. Thus, Cam2p plays a significant role in Myo1p function. However, further studies indicated the existence of an additional Cam2p-binding partner. Cam2p was still present at cortical patches in myo1 cells (or in myo1-IQ2 mutants, which lack an intact Cam2p-binding motif), whereas a cam2 null (cam2) suppressed cytokinesis defects of an essential light chain (ELC) mutant known to be impaired in binding to PI 4-kinase (Pik1p). Binding studies revealed that Cam2p and the ELC compete for Pik1p. Cortical localization of Cam2p in the myo1 background relied on its association with Pik1p, whereas overexpression studies indicated that Cam2p, in turn, contributes to Pik1p function. The fact that the Myo1p-associated defects of a cam2 mutant are more potent than those of a myo1-IQ2 mutant suggests that myosin light chains can contribute to actomyosin function both directly and indirectly (via phospholipid synthesis at sites of polarized growth).

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The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in Saccharomyces cerevisiae

Cited by 110 publications

References 65 publications

The yeast cell cortical protein Num1 integrates mitochondrial dynamics into cellular architecture

The yeast cell cortical protein Num1 integrates mitochondrial dynamics into cellular architecture

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

A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase

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