ArticleNeuroscience letters2008
The actin cross-linking protein AFAP120 regulates axon elongation in a tyrosine phosphorylation-dependent manner.
Article in Neuroscience letters, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Preparation and Characterization of a Polyclonal Antibody against Human Actin Filament-Associated Protein-120 kD.International journal of molecular sciences · 2016Article
- The actin-binding domain of actin filament-associated protein (AFAP) is involved in the regulation of cytoskeletal structure.Cellular and molecular life sciences : CMLS · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Growth cone guidance and axon elongation require the dynamic coordinated regulation of the actin cytoskeleton. As the growth cone moves, actin-dependent forces generate tension that enables protrusive activity in the periphery and drives growth cone translocation. This dynamic remodeling of the actin cytoskeleton in response to membrane tension requires activation of Src kinase. Although it has been proposed that these actin-dependent forces vary with the extent of actin cross-linking, the identity of the cross-linking protein(s) remains unknown. AFAP120 is a nervous system specific actin cross-linking protein that is regulated by Src kinase phosphorylation. Here, we report that AFAP120 is expressed and tyrosine phosphorylated in differentiating cerebellar granule cells, where it is enriched in the axon and growth cone. Over-expression of AFAP120 enhances neurite elongation in a tyrosine phosphorylation-dependent manner. These findings suggest that AFAP120 may coordinate Src signaling with the dynamic changes in the actin cytoskeleton that drive growth cone motility and axon elongation.
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Registered trials
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