Kymolyzer, a Semi‐Autonomous Kymography Tool to Analyze Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

Download Full-text

Batch Fermentation of Recombinant Burkholderia Intracellular Motility A Protein in Escherichia coli for the Diagnosis of Equine Glanders

Journal of Equine Veterinary Science ◽

10.1016/j.jevs.2014.12.009 ◽

2015 ◽

Vol 35 (2) ◽

pp. 124-129 ◽

Cited By ~ 1

Author(s):

Anil K. Singh ◽

Saurabh Shrivastava ◽

Subodh Kumar ◽

Vijai Pal ◽

Nataragan Gopalan

Keyword(s):

Escherichia Coli ◽

Batch Fermentation ◽

Intracellular Motility

Download Full-text

Phosphorylation Modification of Wheat Lectin VER2 Is Associated with Vernalization-Induced O-GlcNAc Signaling and Intracellular Motility

PLoS ONE ◽

10.1371/journal.pone.0004854 ◽

2009 ◽

Vol 4 (3) ◽

pp. e4854 ◽

Cited By ~ 23

Author(s):

Lijing Xing ◽

Juan Li ◽

Yunyuan Xu ◽

Zhihong Xu ◽

Kang Chong

Keyword(s):

Intracellular Motility

Download Full-text

Intracellular motility of mitochondria: role of the inner compartment in migration and shape changes of mitochondria in XTH-cells

Journal of Cell Science ◽

10.1242/jcs.30.1.99 ◽

1978 ◽

Vol 30 (1) ◽

pp. 99-115

Author(s):

J. Bereiter-Hahn

Keyword(s):

Phase Contrast ◽

Heart Cells ◽

Underlying Principle ◽

Good Accord ◽

Contrast Microscopy ◽

Mitochondrial Motility ◽

Time Required ◽

Shape Changes ◽

Intracellular Motility

Mitochondrial movements have been followed by phase-contrast microscopy in living XTH-cells (Xenopus laevis tadpole-heart cells) in tissue culture. The same organelles have been viewed subsequently in electron micrographs. Locomotion of mitochondria proceeds at velocities up to 100 micrometer/min. Formation of branches of mitochondria and other shape changes may occur with the same speed. Mitochondrial motility can be classified into 4 types: (I) Alternating extension and contraction at the two ends of rod-shaped mitochondria. (2) Lateral branching. (3) Alternate stretching and contraction of arbitrary parts of a mitochondrion amounting to a kind of peristaltic action. (4) Transverse wave propagation along the organelle. Types I to 3 can be reduced to the same underlying principle; they cause locomotion. Formation of mitochondrial extensions is due to elongation of cristae. The observations are discussed in terms of 4 specific proposals. (I) Intracellular locomotion of mitochondria is caused by local enlargements and contractions of the organelles. (2) The shape changes are correlated with alterations in the arrangement of the cristae. (3) Such arrangements are not associated with overall swelling or shrinkage of the mitochondrion; they are local features. (4) Estimates of the time required for rearrangement of the inner compartment amount to less than 0.3 s for single crista arrangements during the fastest shape changes, and less than 1–3 s during slower alterations. This high velocity is in good accord with the hypothesis of energy conservation by conformational events during oxidative phosphorylation.

Download Full-text

Macrophage Intracellular Motility and Its Correlation with Cell-Substrate Adhesion

Springer Series in Biophysics - Cytoskeletal and Extracellular Proteins ◽

10.1007/978-3-642-73925-5_43 ◽

1989 ◽

pp. 235-243

Author(s):

Peter Gehr ◽

Samuel Schuerch ◽

Richard Marugg ◽

Marianne Geiser ◽

Vinzenz Im Hof

Keyword(s):

Substrate Adhesion ◽

Cell Substrate ◽

Cell Substrate Adhesion ◽

Intracellular Motility

Download Full-text

Abl Kinases Regulate Actin Comet Tail Elongation via an N-WASP-Dependent Pathway

Molecular and Cellular Biology ◽

10.1128/mcb.25.20.8834-8843.2005 ◽

2005 ◽

Vol 25 (20) ◽

pp. 8834-8843 ◽

Cited By ~ 50

Author(s):

Elizabeth A. Burton ◽

Timothy N. Oliver ◽

Ann Marie Pendergast

Keyword(s):

Host Cell ◽

Actin Polymerization ◽

Shigella Flexneri ◽

Microbial Pathogens ◽

Productive Infection ◽

Cell Protein ◽

Comet Tail ◽

Abl Kinases ◽

Molecular Machinery ◽

Intracellular Motility

ABSTRACT Microbial pathogens have evolved diverse strategies to modulate the host cell cytoskeleton to achieve a productive infection and have proven instrumental for unraveling the molecular machinery that regulates actin polymerization. Here we uncover a mechanism for Shigella flexneri-induced actin comet tail elongation that links Abl family kinases to N-WASP-dependent actin polymerization. We show that the Abl kinases are required for Shigella actin comet tail formation, maximal intracellular motility, and cell-to-cell spread. Abl phosphorylates N-WASP, a host cell protein required for actin comet tail formation, and mutation of the Abl phosphorylation sites on N-WASP impairs comet tail elongation. Furthermore, we show that defective comet tail formation in cells lacking Abl kinases is rescued by activated forms of N-WASP. These data demonstrate for the first time that the Abl kinases play a role in the intracellular motility and intercellular dissemination of Shigella and uncover a new role for Abl kinases in the regulation of pathogen motility.

Download Full-text

Unidirectional Regulation of Vimentin Intermediate Filaments to Caveolin-1

International Journal of Molecular Sciences ◽

10.3390/ijms21207436 ◽

2020 ◽

Vol 21 (20) ◽

pp. 7436

Author(s):

Xuemeng Shi ◽

Changyuan Fan ◽

Yaming Jiu

Keyword(s):

Cell Migration ◽

Stress Response ◽

Intermediate Filaments ◽

Migration Rate ◽

Osmotic Shock ◽

Cellular Level ◽

Caveolin 1 ◽

Active Processes ◽

Intracellular Motility ◽

Vimentin Filaments

Both the mechanosensitive vimentin cytoskeleton and endocytic caveolae contribute to various active processes such as cell migration, morphogenesis, and stress response. However, the crosstalk between these two systems has remained elusive. Here, we find that the subcellular expression between vimentin and caveolin-1 is mutual exclusive, and vimentin filaments physically arrest the cytoplasmic motility of caveolin-1 vesicles. Importantly, vimentin depletion increases the phosphorylation of caveolin-1 on site Tyr14, and restores the compromised cell migration rate and directionality caused by caveolin-1 deprivation. Moreover, upon hypo-osmotic shock, vimentin-knockout recovers the reduced intracellular motility of caveolin-1 vesicles. In contrary, caveolin-1 depletion shows no effect on the expression, phosphorylation (on sites Ser39, Ser56, and Ser83), distribution, solubility, and cellular dynamics of vimentin filaments. Taken together, our data reveals a unidirectional regulation of vimentin to caveolin-1, at least on the cellular level.

Download Full-text