Mechanisms of Intracellular Organelle Transport

Schliwa, Manfred

doi:10.1007/978-1-4684-4592-3_1

Cited by 90 publications

(80 citation statements)

References 319 publications

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“…Most animal cells transport organelles within their cytoplasm (Schliwa, 1984). In neurons, bidirectional organelle transport within axons is thought to be the basis of fast axonal transport (Smith, 1980;Tsukita and Ishikawa, 1980).…”

Section: Introductionmentioning

confidence: 99%

“…These cytoplasmic filaments were identified as single microtubules by electron microscopy and immunofluorescence using antitubulin antibodies (Schnapp et al, 1985). Microtubules also support organelle movements in a variety of nonneuronal cells (Schliwa, 1984;Hayden et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

“…Directed organelle movement within cells depends on ATP (Forman et al, 1984;Schliwa, 1984), and it has been generally assumed that movement is powered by an ATPase. Since all organelles move at the same velocity along isolated microtubules, the same type of molecular motor, or "translocator" may interact with a variety of organelles (Vale et al, 1985a).…”

Section: Introductionmentioning

confidence: 99%

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Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility

Vale

Reese

Sheetz

1985

Cell

1,842

1,182

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SummaryAxoplasm from the squid giant axon contains a soluble protein translocator that induces movement of microtubules on glass, latex beads on microtubules, and axoplasmic organelles on microtubules. We now report the partial purification of a protein from squid giant axons and optic lobes that induces these microtubule-based movements and show that there is a homologous protein in bovine brain. The purification of the translocator protein depends primarily on its unusual property of forming a high affinity complex with microtubules in the presence of a nonhydrolyzable ATP analog, adenylyl imidodiphosphate. The protein, once released from microtubules with ATP, migrates on gel filtration columns with an apparent molecular weight of 600 kilodaltons and contains 110-120 and 60-70 kilodalton polypeptides. This protein is distinct in molecular weight and enzymatic behavior from myosin or dynein, which suggests that it belongs to a novel class of force-generating molecules, for which we propose the name kinesin.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility

Vale

Reese

Sheetz

1985

Cell

1,842

1,182

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“…These filamentous elements turn out to be single microtubules lacking any associated actin or other filaments (24). It is n o w b e c o m i n g increasingly clear that fast axonal transport represents a special case of the more general m e c h a n i s m for organelle transport present in most cells (1,23). In particular, the fast axonal transport of m e mbrane-limited organelles seems to be represented in n o n -n e r v e cells, such as those studied here, as directed or polarized m o v e m e n t of organelles between central a n d peripheral regions of the cytoplasm (20).…”

Section: Discussionmentioning

confidence: 99%

“…The high concentration and spatial organization of filaments in the cytoplasmic meshwork contrasts, however, with the dynamic nature of the cytoplasm observed in living cells (17,20,23,29). It is especially difficult to envision how organelles rapidly move through these dense meshworks, because many organelles are larger than the spaces between filaments.…”

Section: Introductionmentioning

confidence: 95%

The structure of cytoplasm in directly frozen cultured cells. II. Cytoplasmic domains associated with organelle movements.

Bridgman¹,

Kachar²,

Reese³

1986

The Journal of Cell Biology

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Abstract.The relationship between organelle movement and cytoplasmic structure in cultured fibroblasts or epithelial cells was studied using video-enhanced differential interference contrast microscopy and electron microscopy of directly frozen whole mounts. Two functional cytoplasmic domains are characterized by these techniques. A central domain rich in microtubules is associated with directed as well as Brownian movements of organelles, while a surrounding domain rich in f-actin supports directed but often intermittent organelle movements more distally along small but distinct individual microtubule tracks. Differences in the organization of the cytoplasm near microtubules may explain why organelle movements are typically continuous in central regions but usually intermittent along the small tracks through the periphery. The central type of cytoplasm has a looser cytoskeletal meshwork than the peripheral cytoplasm which might, therefore, interfere less frequently with organelles moving along microtubules there.

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