ReviewCurrent protein & peptide science2026
Profilin and Its Isoforms: Unravelling the Functional Diversity Across Life Forms.
Review in Current protein & peptide science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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Authors and funding
2 authors.
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Abstract
The dynamic nature of the cell wall or plasma membrane is extremely important for the various cellular functions. The rearrangement of the cytoskeleton within the cell is a crucial process that is coordinated by the Profilin (PFN) protein. PFN is a small, cytosolic protein whose molecular weight is around 14-17 kDa. Originally, PFN was identified as an actin-binding protein that regulates actin dynamics. However, several studies later reported that the interaction of PFN with certain cytosolic proteins has a role in membrane trafficking, development, motility, and signaling. Additionally, the alternatively spliced PFN isoforms are present in different tissues and govern neurological and developmental functions. A mutation in these isoforms can result in abnormalities in the functioning. These isoforms interact with different ligands with certain specificity. However, the structural and functional biology of these isoforms is still under investigation. This review comprehensively discusses the roles of PFN and its isoforms across diverse species, spanning prokaryotes, eukaryotes, and viruses. Future research efforts are crucial for elucidating novel aspects and enhancing our understanding of the molecular mechanisms governed by PFN and its isoforms.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.