Faculty Opinions recommendation of Kinesin-5 regulates the growth of the axon by acting as a brake on its microtubule array.

2007 ◽  
Author(s):  
Michael Ehlers
Keyword(s):  
Microtubule Array

scholarly journals The rise and fall of the phragmoplast microtubule array

2013 ◽  
Vol 16 (6) ◽  
pp. 757-763 ◽  
Author(s):  
Yuh-Ru Julie Lee ◽  
Bo Liu
Keyword(s):  
Microtubule Array

Microtubules in the Heliozoan Axopodium

1971 ◽  
Vol 8 (1) ◽  
pp. 127-151
Author(s):  
Y. SHIGENAKA ◽  
L. E. ROTH ◽  
D. J. PIHLAJA
Keyword(s):  
Microscopic Study ◽  
Distal Portion ◽  
Distilled Water ◽  
Electron Microscopic ◽  
Reduced Order ◽  
Distal Half ◽  
Microtubule Array ◽  
Proximal Half ◽  
Microtubule Stability ◽  
High Lability

The precise microtubule array present in the heliozoan axopodium has been studied by experimental degradation by using the protein denaturing agent urea. Since concentrations used in typical applications were found to destroy the whole organism immediately, very dilute solutions, usually 0.15 M, were used to study axopodial retraction, which was shown to occur in 2 stages: the distal half reacts immediately and is lost in very few minutes, largely by release of segments, while retraction of the proximal half may extend over an hour. Recovery of axopodial length by removal of organisms to distilled water is possible if treatment is not carried to full axopodium loss, though organisms must be treated with solutions more dilute than 0.1 M to avoid lysis. Electron-microscopic study of retracting axopodia showed degradation of microtubules at innumerable points even in the proximal regions. Similar studies of untreated organisms showed that the typical microtubule array is found throughout the proximal portion but is progressively imprecise in the distal portion as the tip is approached. High lability to urea is therefore correlated with reduced order and reduced numbers of long linkage elements in the microtubule array. An intra-microtubule metastability is proposed and is discussed with regard to the formation of axonemes, the use of dilute urea to test microtubule stability differences, and the gradion hypothesis presented in previous work.

Microtubules facilitate the stimulated secretion of beta-hexosaminidase in lacrimal acinar cells

1998 ◽  
Vol 111 (9) ◽  
pp. 1267-1276 ◽  
Author(s):  
S.R. da Costa ◽  
F.A. Yarber ◽  
L. Zhang ◽  
M. Sonee ◽  
S.F. Hamm-Alvarez
Keyword(s):  
Confocal Microscopy ◽  
Cytochalasin D ◽  
Apical Plasma Membrane ◽  
Secretory Proteins ◽  
Apical Region ◽  
Cell Periphery ◽  
Isolated Cells ◽  
Microtubule Array ◽  
Lacrimal Acinar Cells

Stimulation of lacrimal acini with secretagogues such as carbachol initiates movement and fusion of acinar secretory vesicles with the apical plasma membrane, resulting in release of protein into the nascent tear fluid. Using rabbit lacrimal acini reconstituted in vitro from isolated cells, we have investigated the organization of the apical cytoskeleton and its role in stimulated secretion. Confocal microscopy revealed a microtubule array emanating from the apical region of the acini; the apical region was also enriched in microfilaments and (gamma)-tubulin. Cytokeratin-based intermediate filaments were apically concentrated, and also detected at the cell periphery. Neither confocal microscopy nor biochemical analysis revealed any reorganization of lumenal microfilaments or microtubules which might accompany carbachol-stimulated release of secretory proteins. However, major changes in the acinar microtubule array induced by taxol or nocodazole were correlated with inhibition of carbachol-dependent release of the secreted protein, beta-hexosaminidase. Major changes in lumenal microfilaments induced by jasplakinolide or cytochalasin D did not inhibit the carbachol-dependent release of beta-hexosaminidase; rather, release of beta-hexosaminidase from jasplakinolide- or cytochalasin D-treated carbachol-stimulated acini was markedly increased relative to the release from untreated stimulated acini. Our findings demonstrate that microtubules play a major role in stimulated lacrimal secretion, and suggest a contributory role for microfilaments.

scholarly journals The organization of Golgi in Drosophila bristles requires microtubule motor protein function and a properly organized microtubule array

PLoS ONE ◽  
2019 ◽  
Vol 14 (10) ◽  
pp. e0223174
Author(s):  
Anna Melkov ◽  
Raju Baskar ◽  
Rotem Shachal ◽  
Yehonathan Alcalay ◽  
Uri Abdu
Keyword(s):  
Protein Function ◽  
Motor Protein ◽  
Microtubule Array ◽  
Microtubule Motor ◽  
Microtubule Motor Protein

MAPs: cellular navigators for microtubule array orientations in Arabidopsis

2013 ◽  
Vol 33 (1) ◽  
pp. 1-21 ◽  
Author(s):  
Sylwia Struk ◽  
Pankaj Dhonukshe
Keyword(s):  
Microtubule Array
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