Towards a new classification of intracellular particle movements based on quantitative analyses

Weiss, Dieter G.; Keller, Franz; Gulden, Josef; Maile, Willi

doi:10.1002/cm.970060210

Cited by 29 publications

(18 citation statements)

References 27 publications

(32 reference statements)

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“…Indeed, when Weiss et al (1986) compared various types of intracellular organelle motility by quantitative motion analysis, they found that "interrupted motion type II" (pauses and direction reversals) is typical for larger organelles, such as lysosomes in cultured cells.…”

Section: Discussionmentioning

confidence: 99%

Myosin Va Bound to Phagosomes Binds to F-Actin and Delays Microtubule-dependent Motility

Al-Haddad

Shonn

Redlich

et al. 2001

MBoC

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We established a light microscopy-based assay that reconstitutes the binding of phagosomes purified from mouse macrophages to preassembled F-actin in vitro. Both endogenous myosin Va from mouse macrophages and exogenous myosin Va from chicken brain stimulated the phagosome-F-actin interaction. Myosin Va association with phagosomes correlated with their ability to bind F-actin in an ATP-regulated manner and antibodies to myosin Va specifically blocked the ATP-sensitive phagosome binding to F-actin. The uptake and retrograde transport of phagosomes from the periphery to the center of cells in bone marrow macrophages was observed in both normal mice and mice homozygous for the dilute-lethal spontaneous mutation (myosin Va null). However, in dilute-lethal macrophages the accumulation of phagosomes in the perinuclear region occurred twofold faster than in normal macrophages. Motion analysis revealed saltatory phagosome movement with temporarily reversed direction in normal macrophages, whereas almost no reversals in direction were observed in dilute-lethal macrophages. These observations demonstrate that myosin Va mediates phagosome binding to F-actin, resulting in a delay in microtubuledependent retrograde phagosome movement toward the cell center. We propose an "antagonistic/cooperative mechanism" to explain the saltatory phagosome movement toward the cell center in normal macrophages.

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Section: Discussionmentioning

confidence: 99%

Myosin Va Bound to Phagosomes Binds to F-Actin and Delays Microtubule-dependent Motility

Al-Haddad

Shonn

Redlich

et al. 2001

MBoC

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“…Motion analysis of organelle movement along individual microtubules was performed as described using the software packages PARTI-MOVI or SPSS (23,25).…”

Section: Methodsmentioning

confidence: 99%

The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport

Waterman‐Storer

Karki

Kuznetsov

et al. 1997

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

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231

161

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Fast axonal transport is characterized by the bidirectional, microtubule-based movement of membranous organelles. Cytoplasmic dynein is necessary but not sufficient for retrograde transport directed from the synapse to the cell body. Dynactin is a heteromultimeric protein complex, enriched in neurons, that binds to both microtubules and cytoplasmic dynein. To determine whether dynactin is required for retrograde axonal transport, we examined the effects of anti-dynactin antibodies on organelle transport in extruded axoplasm. Treatment of axoplasm with antibodies to the p150 Glued subunit of dynactin resulted in a significant decrease in the velocity of microtubule-based organelle transport, with many organelles bound along microtubules. We examined the molecular mechanism of the observed inhibition of motility, and we demonstrated that antibodies to p150 Glued disrupted the binding of cytoplasmic dynein to dynactin and also inhibited the association of cytoplasmic dynein with organelles. In contrast, the anti-p150 Glued antibodies had no effect on the binding of dynactin to microtubules nor on cytoplasmic dynein-driven microtubule gliding. These results indicate that the interaction between cytoplasmic dynein and the dynactin complex is required for the axonal transport of membrane-bound vesicles and support the hypothesis that dynactin may function as a link between the organelle, the microtubule, and cytoplasmic dynein during vesicle transport.Neurons possess a striking asymmetric morphology in which elongated axonal processes extend from the cell body. The growth and maintenance of the axon, as well as the movement of materials between the cell body and the distal tip of the axon, rely on the mechanism of axonal transport. The fast bidirectional transport of organelles along the polarized microtubule array of the axon has been well characterized (1-8). Many microtubule-based motors have been identified in neurons, including members of the kinesin superfamily that are implicated in anterograde transport (4, 5) and cytoplasmic dynein, which is required for retrograde transport (6-8).The molecular mechanisms by which these motors are specified for particular types of organelle cargo, as well as the regulation of the interactions between motor proteins, organelles, and microtubules, are largely unknown. A soluble accessory factor, dynactin, was originally isolated via its copurification with cytoplasmic dynein and is one candidate for the activation of cytoplasmic dynein-based organelle motility (reviewed in ref. 9). Dynactin consists of at least seven different polypeptides that cosediment at 20 S (10, 11). These include p150Glued ; the actin-related protein centractin (Arp-1); the ␣ and ␤ subunits of capping protein (CapZ); dynamitin; as well as uncharacterized polypeptides with molecular masses of 62 and 24 kDa (10-17). The largest dynactin polypeptide, p150Glued , is capable of multiple, specific binding interactions. p150Glued binds to the 74-kDa intermediate chain of cytoplasmic dynein via a domain ...

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“…Only occasionally were vesicles observed in close proximity to the cell wall, and these vesicles moved in various directions and with changing velocities in the plane of the plasma membrane as if they were following invisible tracks. Such saltatory movements (interrupted type I according to Weiss et al [1986]) were typical for wounded regions that lacked thick actin filament bundles and/or active unidirectional displacement of organelles. Saltatory movements alternated with trembling or oscillating motions, probably of the Brownian type.…”

Section: Vesicle Dynamics and Organisation Of The Actin Cytoskeletonmentioning

confidence: 99%

Actin-based vesicle dynamics and exocytosis during wound wall formation in characean internodal cells

Foissner

Lichtscheidl

Wasteneys

1996

Cell Motil. Cytoskeleton

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Towards a new classification of intracellular particle movements based on quantitative analyses

Cited by 29 publications

References 27 publications

Myosin Va Bound to Phagosomes Binds to F-Actin and Delays Microtubule-dependent Motility

Myosin Va Bound to Phagosomes Binds to F-Actin and Delays Microtubule-dependent Motility

The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport

Actin-based vesicle dynamics and exocytosis during wound wall formation in characean internodal cells

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