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

Bridgman, Paul C.; Kachar, Bechara; Reese, Thomas S.

doi:10.1083/jcb.102.4.1510

Cited by 48 publications

(32 citation statements)

References 31 publications

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“…Blebbistatin effects on actin flow in the growth cone neck were accompanied by significant spreading of the C domain and associated organelles (Bridgman et al, 1986; Figures 3C, 3F, and 3L). However, spreading was never observed in more proximal regions of the neurite shaft, suggesting these regions had undergone some kind of stabilization (Figure 3L).…”

Section: Resultsmentioning

confidence: 99%

Myosin II Activity Facilitates Microtubule Bundling in the Neuronal Growth Cone Neck

et al. 2008

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SUMMARY The cell biological processes underlying axon growth and guidance are still not well understood. An outstanding question is how a new segment of the axon shaft is formed in the wake of neuronal growth cone advance. For this to occur, the highly dynamic, splayed-out microtubule (MT) arrays characteristic of the growth cone must be consolidated (bundled together) to form the core of the axon shaft. MT-associated proteins stabilize bundled MTs, but how individual MTs are brought together for initial bundling is unknown. Here, we show that laterally moving actin arcs, which are myosin II-driven contractile structures, interact with growing MTs and transport them from the sides of the growth cone into the central domain. Upon Myosin II inhibition, the movement of actin filaments and MTs immediately stopped and MTs unbundled. Thus, Myosin II-dependent compressive force is necessary for normal MT bundling in the growth cone neck.

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Section: Resultsmentioning

confidence: 99%

Myosin II Activity Facilitates Microtubule Bundling in the Neuronal Growth Cone Neck

et al. 2008

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“…In other systems, organelles not only co-localize with microtubules, microfilaments, and intermediate filaments (Hirokawa, 1982;Bridgmen et al, 1986;Menzel and Schliwa, 1986) but move along microtubules Brady et al, 1982;Hayden and Allen, 1984;Koonce and Schliwa, 1985) and microfilaments (Kachar, 1985;Adams and Pollard, 1986;Kachar and Reese, 1988;Kohno and Shimmen, 1988;Hegmann et al, 1989Hegmann et al, , 1991Wessels et al, 1989;Kuznetsov et al, 1992). Motor molecules, which are cytoskeleton-associated ATPases, drive this organellar movement (Pollard et al, 1991; reviewed by Schroer and Sheetz, 1991;Titus, 1993).…”

Section: Introductionmentioning

confidence: 95%

Organelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae.

Smith

Simon

O'Sullivan

et al. 1995

MBoC

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During early stages of meiosis I, yeast mitochondria fuse to form a single continuous thread. Thereafter, portions of the mitochondrial thread are equally distributed to daughter cells. Using time-lapse fluorescence microscopy and a membrane potential sensing dye, mitochondria are resolved as small particles at the cell periphery in pre-meiotic, living yeast. These organelles display low levels of movement. During meiosis I, we observed a threefold increase in mitochondrial motility. Mitochondrial movements were linear, occurred at a maximum velocity of 25 +/- 6.7 nm/s, and resulted in organelle collision and fusion to form elongated tubular structures. Mitochondria do not co-localize with microtubules. Destabilization of microtubules by nocodazole treatment has no significant effect on the rate and extent of thread formation. In contrast, yeast bearing temperature-sensitive mutations in the actin-encoding ACT1 gene (act1-3 and act1-133) exhibit abnormal mitochondrial aggregation, fragmentation, and enlargement as well as loss of mitochondrial motility. In act1-3 cells, mitochondrial defects and actin delocalization occur only at restrictive temperatures. The act1-133 mutation, which perturbs the myosin-binding site of actin without significantly affecting actin cytoskeletal structure in meiotic yeast, results in mitochondrial morphology and motility defects at restrictive and permissive temperatures. These studies support a role for the actin cytoskeleton in the control of mitochondrial position and movements in meiotic yeast.

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“…Individual organelles or groups of several organelles linked together sometimes ventured into the P domain along linear trajectories; however, such events were infrequent, isolated, and transient. Many organelles appeared to reverse their direction of transport in the transition zone between the C and P domains, as if a physical barrier to transport existed at the C-P domain interface (see Vale et al, 1985~;Bridgman et al, 1986). Organelles sometimes moved several microns into the P domain and then reversed direction, returning to the C domain.…”

Section: Central and Peripheral Domains In Growth Conesmentioning

confidence: 99%

“…When observed in video-enhanced DIC microscopy, organelle movement along bag cell neurites or axons has an organized, linear character, probably as a result of translocation along microtubules (Allen et al, 1985;Koonce and Schliwa, 1985;Bridgman et al, 1986; see Schnapp and Reese, 1986, for a review). Organelles move into and out of growth cones under control conditions; however, transport is restricted mostly to the growth cone core, which represents the most distal extension of the C domain.…”

Section: Central and Peripheral Domains In Growth Conesmentioning

confidence: 99%

“…To distinguish between the different forms of motility we observe in growth cone cores and lamellae, we will adopt the central (C) versus peripheral (P) cytoplasmic domain convention proposed by Bridgman et al (1986). Aplysia neuron growth cone cores have C domain characteristics-high organelle and microtubule density-and exhibit continuous, directed organelle movements.…”

Section: Central and Peripheral Domains In Growth Conesmentioning

confidence: 99%

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Cyclic AMP induces changes in distribution and transport of organelles within growth cones of Aplysia bag cell neurons

et al. 1987

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This report examines cAMP-induced regulation of directed organelle transport in bag cell neuron growth cones using video-enhanced differential interference contrast (DIC) microscopy (Allen et al., 1981; Inoue, 1981) and digital image analysis techniques. Under control conditions, organelle transport is evident in the central cytoplasmic regions of bag cell neuron growth cones, but not in lamellae. Motility of lamellae takes the form of slow (less than 0.01 micron/sec) extension of margins and ruffling motions that propagate as waves (velocity, approximately 0.07 micron/sec) in a retrograde direction. Application of forskolin and a phosphodiesterase (PDE) inhibitor at concentrations known to induce changes in bag cell protein phosphorylation resulted in (1) rapid extension of directed organelle transport into lamellae, and (2) inhibition of the retrograde ruffling waves. These changes effected transformation of lamellae into neurite endings packed with microtubules and organelles, a large proportion of which appeared to be neurosecretory granules. The effects were reversible, dose-dependent, potentiated by a variety of PDE inhibitors, and mimicked by 6-N-butyl-8-benzyl-thio-cAMP (BT-cAMP). Though forskolin may normally promote depolarization and Ca entry, these changes in growth cone structure are not secondary to influx of external Ca, as they persist in Ca-free/EGTA solutions; furthermore, they do not resemble the effects of depolarization induced by perfusion with elevated K solutions. The cAMP-induced changes in growth cone morphology that we report here suggest a possible role for protein phosphorylation in promoting growth cone differentiation and structural changes accompanying secretion.

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

Cited by 48 publications

References 31 publications

Myosin II Activity Facilitates Microtubule Bundling in the Neuronal Growth Cone Neck

Myosin II Activity Facilitates Microtubule Bundling in the Neuronal Growth Cone Neck

Organelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae.

Cyclic AMP induces changes in distribution and transport of organelles within growth cones of Aplysia bag cell neurons

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