Effects of Mechanical Strain on Structural and Actin-Binding Proteins in Neuroblasts

Mechanical stimulation affects the functioning and outgrowth of neurons and has the potential capacity for regeneration. Mechanoreceptors in sensory neurons act as a conduit to respond to pain and touch while neurites experience mechanical stimulation during the process of animal growth. To understand mechanotransduction in neural outgrowth, we used a custom fabricated device to investigate the effects of static mechanical stretching while examining molecular connections such as advillin and actin. Our results have the potential of providing greater understanding of mechanotransduction in neuroblasts, as well as providing insight into mechanical approaches that might be used in increasing neural outgrowth.

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High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100122964 ◽

1992 ◽

Vol 50 (1) ◽

pp. 512-513

Author(s):

J. Jakana ◽

M.F. Schmid ◽

P. Matsudaira ◽

W. Chiu

Keyword(s):

High Resolution ◽

Binding Proteins ◽

Actin Binding ◽

Eukaryotic Cells ◽

Dimensional Structure ◽

Structural Basis ◽

Actin Bundle ◽

Actin Bundles ◽

3 Dimensional ◽

Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

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Faculty Opinions recommendation of Expression of actin-binding proteins and requirement for actin-depolymerizing factor in chick neural crest cells.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.718468444.793502361 ◽

2014 ◽

Author(s):

Paul Kulesa

Keyword(s):

Neural Crest ◽

Binding Proteins ◽

Neural Crest Cells ◽

Actin Binding ◽

Actin Depolymerizing Factor ◽

Actin Binding Proteins

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Actin-binding proteins sensitively mediate actin bundle stiffness

Journal of Biomechanics ◽

10.1016/s0021-9290(06)83904-7 ◽

2006 ◽

Vol 39 ◽

pp. S240

Author(s):

M. Bathe ◽

M. Claessens ◽

E. Frey ◽

A. Bausch

Keyword(s):

Binding Proteins ◽

Actin Binding ◽

Actin Binding Proteins ◽

Actin Bundle

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Exploration of Alternative Splicing Events in Mesenchymal Stem Cells from Human Induced Pluripotent Stem Cells

Genes ◽

10.3390/genes12050737 ◽

2021 ◽

Vol 12 (5) ◽

pp. 737

Author(s):

Ji-Eun Jeong ◽

Binna Seol ◽

Han-Seop Kim ◽

Jae-Yun Kim ◽

Yee-Sook Cho

Keyword(s):

Stem Cells ◽

Mesenchymal Stem Cells ◽

Alternative Splicing ◽

Functional Enrichment ◽

Actin Binding ◽

Pcr Analysis ◽

Valuable Insight ◽

Sequencing Analysis ◽

Induced Pluripotent ◽

Insight Into

Although comparative genome-wide transcriptomic analysis has provided insight into the biology of human induced pluripotent stem cell-derived mesenchymal stem cells (iMSCs), the distinct alternative splicing (AS) signatures of iMSCs remain elusive. Here, we performed Illumina RNA sequencing analysis to characterize AS events in iMSCs compared with tissue-derived MSCs. A total of 4586 differentially expressed genes (|FC| > 2) were identified between iMSCs and umbilical cord blood-derived MSCs (UCB-MSCs), including 2169 upregulated and 2417 downregulated genes. Of these, 164 differentially spliced events (BF > 20) in 112 genes were identified between iMSCs and UCB-MSCs. The predominant type of AS found in iMSCs was skipped exons (43.3%), followed by retained introns (19.5%), alternative 3′ (15.2%) and 5′ (12.8%) splice sites, and mutually exclusive exons (9.1%). Functional enrichment analysis showed that the differentially spliced genes (|FC| > 2 and BF > 20) were mainly enriched in functions associated with focal adhesion, extracellular exosomes, extracellular matrix organization, cell adhesion, and actin binding. Splice isoforms of selected genes including TRPT1, CNN2, and AP1G2, identified in sashimi plots, were further validated by RT-PCR analysis. This study provides valuable insight into the biology of iMSCs and the translation of mechanistic understanding of iMSCs into therapeutic applications.

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Control of microtubule dynamics using an optogenetic microtubule plus end–F-actin cross-linker

The Journal of Cell Biology ◽

10.1083/jcb.201705190 ◽

2017 ◽

Vol 217 (2) ◽

pp. 779-793 ◽

Cited By ~ 9

Author(s):

Rebecca C. Adikes ◽

Ryan A. Hallett ◽

Brian F. Saway ◽

Brian Kuhlman ◽

Kevin C. Slep

Keyword(s):

Blue Light ◽

Actin Binding ◽

Cross Linking ◽

Dependent Manner ◽

Exclusion Zone ◽

Actin Networks ◽

Drosophila Melanogaster S2 Cells ◽

Actin Binding Domain ◽

Specific Factors ◽

Insight Into

We developed a novel optogenetic tool, SxIP–improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein–dependent manner using blue light. We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation. We used this system to investigate the effects of cross-linking MT plus ends and F-actin in Drosophila melanogaster S2 cells to gain insight into spectraplakin function and mechanism. We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks. Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone. SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

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