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Updated: Apr 27, 2026

A Simplified and Efficient Method to Isolate Primary Human Keratinocytes from Adult Skin Tissue
Published on: August 25, 2018
FYNagling divergent adhesive functions for Fyn in keratinocytes
Sarah E Fenton1, Mitchell F Denning
1Molecular Biology Program, Cardinal Bernardin Cancer Center, Loyola University Chicago, Maywood, IL, USA.
Abstract:
Fyn, a member of the Src family kinases (SFKs), has been shown to play important yet contradictory roles in keratinocyte (KC) adhesion. During KC differentiation, physiological activation of Fyn results in the formation of adherens junctions, recruiting junctional components and inducing signaling pathways that control the differentiation program. However, in KC transformation and oncogenesis, increased Fyn activity has been implicated in the dissolution of adhesion structures and an increased migratory phenotype. Fyn activity is also associated with both the formation and dissolution of focal adhesions, and to a lesser extent hemidesmosomes and desmosomes. This viewpoint article aims to reconcile these disparate bodies of literature regarding Fyn's role in cell-cell and cell-matrix adhesion by proposing several alternative, testable hypotheses that unify Fyn's fractured functions.
Insights
Fyn kinase has dual roles in keratinocyte (KC) adhesion, promoting it during differentiation but hindering it in cancer. This review proposes hypotheses to unify Fyn's contradictory functions in cell adhesion.
Area of Science:
- Cell Biology
- Biochemistry
- Dermatology
Background:
- Fyn, a Src family kinase (SFK), exhibits paradoxical roles in keratinocyte (KC) adhesion.
- Physiological Fyn activation supports KC differentiation and adherens junction formation.
- Aberrant Fyn activity in cancer is linked to adhesion loss and increased migration.
Purpose of the Study:
- To reconcile conflicting literature on Fyn's function in KC cell-cell and cell-matrix adhesion.
- To propose unifying hypotheses for Fyn's diverse roles in keratinocyte adhesion dynamics.
- To provide testable hypotheses for future research into Fyn's regulatory mechanisms.
Main Methods:
- Literature review and synthesis of existing research on Fyn kinase.
- Analysis of Fyn's involvement in various adhesion structures (adherens junctions, focal adhesions, desmosomes, hemidesmosomes).
- Development of theoretical frameworks to explain Fyn's context-dependent functions.
Main Results:
- Fyn's activity is context-dependent, influencing different adhesion types.
- Fyn can both promote and inhibit adhesion complex formation and stability.
- Fyn's role varies significantly between normal differentiation and oncogenic transformation.
Conclusions:
- Fyn's seemingly contradictory roles in keratinocyte adhesion can be explained by context-specific mechanisms.
- Further research is needed to elucidate the precise molecular pathways mediating Fyn's dual functions.
- Understanding Fyn's regulation is crucial for targeting keratinocyte-related diseases and cancer progression.
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