Studying Axoplasmic Transport by Video Microscopy and Using the Squid Giant Axon as a Model System

Weiss, Dieter G.; Meyer, Monica A.; Langford, George M.

doi:10.1007/978-1-4899-2489-6_15

Cited by 12 publications

(4 citation statements)

References 93 publications

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“…In the case o f gliding the kinesin molecules are attached to the glass surface perhaps in an unspecific way and may even be partially denatured. In the case of vesicle transport the confor mational state of kinesin may be well defined and determined by its interaction with specific receptors or perhaps with dynein residing nearby at the organelle membrane (compare Brady et al. 1990;Sheetz et al this volume).…”

Section: Resultsmentioning

confidence: 99%

Characteristics of the motor responsible for the gliding of native microtubules from squid axoplasm

Weiss

Seitz‐Tutter

Langford

1991

Journal of Cell Science

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Section: Resultsmentioning

confidence: 99%

Characteristics of the motor responsible for the gliding of native microtubules from squid axoplasm

Weiss

Seitz‐Tutter

Langford

1991

Journal of Cell Science

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“…The mechanisms of slow and fast axon transport have been extensively studied in the squid giant fiber system (Weiss et al, 1990). Originally, it was believed that neurofilaments were transported as part of the slow transport system, along with tubulin and actin.…”

Section: A Model Of Topographic Regulation Of Nf Protein Phosphorylatmentioning

confidence: 99%

Squid (Loligo pealei) Giant Fiber System: A Model for Studying Neurodegeneration and Dementia?

Grant

Zheng

Pant

2006

The Biological Bulletin

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Abstract. In many neurodegenerative disorders that lead to memory loss and dementia, the brain pathology responsible for neuronal loss is marked by accumulations of proteins in the form of extracellular plaques and intracellular filamentous tangles, containing hyperphosphorylated cytoskeletal proteins. These are assumed to arise as a consequence of deregulation of a normal pattern of topographic phosphorylation-that is, an abnormal shift of cytoskeletal protein phosphorylation from the normal axonal compartment to cell bodies. Although decades of studies have been directed to this problem, biochemical approaches in mammalian systems are limited: neurons are too small to permit separation of cell body and axon compartments. Since the pioneering studies of Hodgkin and Huxley on the giant fiber system of the squid, however, the stellate ganglion and its giant axons have been the focus of a large literature on the physiology and biochemistry of neuron function. This review concentrates on a host of studies in our laboratory and others on the factors regulating compartment-specific patterns of cytoskeletal protein phosphorylation (primarily neurofilaments) in an effort to establish a normal baseline of information for further studies on neurodegeneration. On the basis of these data, a model of topographic regulation is proposed that offers several possibilities for further studies on potential sites of deregulation that may lead to pathologies resembling those seen in mammalian and human brains showing neurodegeneration, dementia, and neuronal cell death.

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“…Giant axons were dissected from freshly caught squid, placed in filtered seawater, and then finely dissected in Ca 2ϩ -free seawater. After fine dissection, axoplasm was extruded from the giant axon onto a microscope slide as previously described (Allen et al, 1985;Weiss et al, 1990). Immediately following the extrusion of axoplasm, 20 L TAMD buffer (25 mM Tris, 5 mM ATP, 5 mM MgCl 2 , 2 mM DTT, pH 7.5, in UltraPure dH 2 O) with 1 M rhodamine-phalloidin (Molecular Probes) was added to each slide.…”

Section: Motility Assays From Squid Axoplasmmentioning

confidence: 99%

Short‐range axonal/dendritic transport by myosin‐V: A model for vesicle delivery to the synapse

2003

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Myosin-V is a versatile motor involved in short-range axonal/dendritic transport of vesicles in the actin-rich cortex and synaptic regions of nerve cells. It binds to several different kinds of neuronal vesicles by its globular tail domain but the mechanism by which it is recruited to these vesicles is not known. In this study, we used an in vitro motility assay derived from axoplasm of the squid giant axon to study the effects of the globular tail domain on the transport of neuronal vesicles. We found that the globular tail fragment of myosin-V inhibited actin-based vesicle transport by displacing native myosin-V and binding to vesicles. The globular tail domain pulled down kinesin, a known binding partner of myosin-V, in affinity isolation experiments. These data confirmed earlier evidence that kinesin and myosin-V interact to form a hetero-motor complex. The formation of a kinesin/myosin-V hetero-motor complex on vesicles is thought to facilitate the coordination of long-range movement on microtubules and short-range movement on actin filaments. The direct interaction of motors from both filament systems may represent the mechanism by which the transition of vesicles from microtubules to actin filaments is regulated. These results are the first demonstration that the recombinant tail of myosin-V inhibits vesicle transport in an in vitro motility assay. Future experiments are designed to determine the functional significance of the interaction between myosin-V and kinesin and to identify other proteins that bind to the globular tail domain of myosin-V.

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Studying Axoplasmic Transport by Video Microscopy and Using the Squid Giant Axon as a Model System

Cited by 12 publications

References 93 publications

Characteristics of the motor responsible for the gliding of native microtubules from squid axoplasm

Characteristics of the motor responsible for the gliding of native microtubules from squid axoplasm

Squid (Loligo pealei) Giant Fiber System: A Model for Studying Neurodegeneration and Dementia?

Short‐range axonal/dendritic transport by myosin‐V: A model for vesicle delivery to the synapse

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