scholarly journals Abl signaling directs growth of a pioneer axon in Drosophila by shaping the intrinsic fluctuations of actin

2020 ◽  
Vol 31 (6) ◽  
pp. 466-477
Author(s):  
Akanni Clarke ◽  
Philip G. McQueen ◽  
Hsiao Yu Fang ◽  
Ramakrishnan Kannan ◽  
Victor Wang ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Growth Cone ◽  
Distal Part ◽  
Forward Bias ◽  
Live Imaging ◽  
Axon Extension ◽  
Abl Tyrosine Kinase ◽  
Intrinsic Fluctuations

Live imaging reveals that a forward bias of the stochastic actin fluctuations in the distal part of an axon drives axon extension by advancing the protrusive, filopodial domain of the growth cone. The actin mass is itself shaped by guidance signaling via Abl tyrosine kinase, which regulates growth cone length and minimizes its disorder.

scholarly journals Abl signaling shapes the intrinsic fluctuations of actin to direct growth of a pioneer axon in Drosophila

2019 ◽  
Author(s):  
Akanni Clarke ◽  
Philip G. McQueen ◽  
Hsiao Yu Fang ◽  
Ramakrishnan Kannan ◽  
Victor Wang ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Growth Cone ◽  
Fundamental Problem ◽  
Forward Bias ◽  
Axon Growth ◽  
Abl Tyrosine Kinase ◽  
Intrinsic Fluctuations ◽  
Direct Growth ◽  
Directed Growth ◽  
Internal Coherence

AbstractThe fundamental problem in axon growth and guidance is to understand how cytoplasmic signaling modulates the cytoskeleton to produce directed growth cone motility. We show here that the TSM1 pioneer axon of Drosophila extends by using Abl tyrosine kinase to shape the intrinsic fluctuations of a mass of accumulated actin in the distal axon. The actin mass fluctuates stochastically in length, but with a small, forward bias that drives the axon along its trajectory by promoting emergence of protrusions in leading intervals where actin accumulates, and collapse of protrusions in lagging intervals that actin has vacated. The actin mass is sculpted by Abl signaling, which probabilistically modulates its key parameters - its width and internal disorder - to drive its advance, while maintaining internal coherence. Comparison of TSM1 to other systems suggests that the mechanism we demonstrate here is apt to be common among pioneer axons in many organisms.

scholarly journals Dynamic morphogenesis of a pioneer axon in Drosophila and its regulation by Abl tyrosine kinase

2020 ◽  
Vol 31 (6) ◽  
pp. 452-465 ◽  
Author(s):  
Akanni Clarke ◽  
Philip G. McQueen ◽  
Hsiao Yu Fang ◽  
Ramakrishnan Kannan ◽  
Victor Wang ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Live Imaging ◽  
Morphological Properties ◽  
Native Tissue ◽  
Abl Tyrosine Kinase

Live imaging of an axon in its native tissue shows that its growth is protrusive and occurs by stabilization of selected filopodia. Guidance signaling, however, for example, via Abl tyrosine kinase, does not control these morphological properties directly but rather controls actin distribution to determine where filopodial dynamics can occur.

scholarly journals SH2-containing phosphotyrosine phosphatase Syp is a target of p210bcr-abl tyrosine kinase.

1994 ◽  
Vol 269 (21) ◽  
pp. 15381-15387 ◽  
Author(s):  
T. Tauchi ◽  
G.S. Feng ◽  
R. Shen ◽  
H.Y. Song ◽  
D. Donner ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Phosphotyrosine Phosphatase ◽  
Abl Tyrosine Kinase

scholarly journals Activation of the Cytoplasmic c-Abl Tyrosine Kinase by Reactive Oxygen Species

2000 ◽  
Vol 275 (23) ◽  
pp. 17237-17240 ◽  
Author(s):  
Xiangao Sun ◽  
Pradip Majumder ◽  
Hisashi Shioya ◽  
Frank Wu ◽  
Shailendra Kumar ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Tyrosine Kinase ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Abl Tyrosine Kinase

scholarly journals Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor.

1991 ◽  
Vol 88 (13) ◽  
pp. 5927-5931 ◽  
Author(s):  
A. M. Pendergast ◽  
A. J. Muller ◽  
M. H. Havlik ◽  
R. Clark ◽  
F. McCormick ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Abl Tyrosine Kinase

scholarly journals Interaction of theN-Methyl-d-Aspartic Acid Receptor NR2D Subunit with the c-Abl Tyrosine Kinase

2000 ◽  
Vol 275 (17) ◽  
pp. 12725-12729 ◽  
Author(s):  
Robert T. Glover ◽  
Maria Angiolieri ◽  
Steven Kelly ◽  
Daniel T. Monaghan ◽  
Jean Y. J. Wang ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Aspartic Acid ◽  
Acid Receptor ◽  
Abl Tyrosine Kinase

A novel mechanism for BCR-ABL action: stimulated secretion of CCN3 is involved in growth and differentiation regulation

Blood ◽  
2006 ◽  
Vol 108 (5) ◽  
pp. 1716-1723 ◽  
Author(s):  
Lynn McCallum ◽  
Susan Price ◽  
Nathalie Planque ◽  
Bernard Perbal ◽  
Andrew Pierce ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Direct Consequence ◽  
Suppressor Gene ◽  
Hematopoietic Stem ◽  
Protein Levels ◽  
Abl Kinase ◽  
Abl Tyrosine Kinase ◽  
Ccn3 Expression

Chronic myeloid leukemia (CML) is characterized by the presence of the constitutively active BCR-ABL protein tyrosine kinase. Using a multipotent hemopoietic cell line, FDCP-Mix, expressing BCR-ABL tyrosine kinase, we investigated the initial effects of this kinase in primitive hematopoietic stem cells. We identified down-regulation of a novel gene, CCN3, as a direct consequence of BCR-ABL kinase activity. CCN3 has been reported to function as a tumor suppressor gene in solid tumors. Northern and Western blotting plus immunocytochemical analysis confirmed CCN3 expression is decreased and is tyrosine-phosphorylated in BCR-ABL kinase active FDCP-Mix cells. Decreased cellular CCN3 correlated with increased CCN3 secretion in BCR-ABL kinase active cells. In vitro treatment of human CML cell lines with imatinib or siRNA directed against BCR-ABL significantly reduced BCR-ABL while increasing CCN3 expression. Cells from patients responding to imatinib showed a similar decrease in BCR-ABL and increase in CCN3. CML CD34+ cells treated with imatinib in vitro demonstrated increased CCN3 protein. Transfecting CCN3 into BCR-ABL+ cells inhibited proliferation and decreased clonogenic potential. CCN3 plays an important role in internal and external cell-signaling pathways. Thus, BCR-ABL can regulate protein levels by governing secretion, a novel mechanism for this tyrosine kinase.

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