Fimbrin

PLS1
Identifiers
Aliases	PLS1, Fimbrin, plastin 1, DFNA76
External IDs	OMIM: 602734 MGI: 104809 HomoloGene: 68270 GeneCards: PLS1
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q23 Start 142,596,393 bp[1] End 142,713,664 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 E3.3 Start 95,634,695 bp[2] End 95,727,364 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte jejunal mucosa rectum duodenum palpebral conjunctiva bronchial epithelial cell islet of Langerhans gallbladder pancreatic epithelial cell pancreatic ductal cell Top expressed in intestinal villus ileum jejunum duodenum large intestine left colon pyloric antrum yolk sac epithelium of stomach utricle More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding actin binding structural constituent of cytoskeleton metal ion binding actin filament binding Cellular component terminal web extracellular exosome brush border cytoplasm actin filament actin filament bundle Biological process intestinal D-glucose absorption regulation of microvillus length terminal web assembly positive regulation of multicellular organism growth actin filament bundle assembly actin filament network formation actin crosslink formation positive regulation of protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5357 102502 Ensembl ENSG00000120756 ENSMUSG00000049493 UniProt Q14651 Q3V0K9 RefSeq (mRNA) NM_001145319 NM_001172312 NM_002670 NM_001033210 RefSeq (protein) NP_001138791 NP_001165783 NP_002661 NP_001028382 Location (UCSC) Chr 3: 142.6 – 142.71 Mb Chr 9: 95.63 – 95.73 Mb PubMed search [3] [4]
Wikidata
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Fimbrin also known as is plastin 1 is a protein that in humans is encoded by the PLS1 gene.^[5] Fimbrin is an actin cross-linking protein important in the formation of filopodia.

Structure

Fimbrin belongs to the calponin homology (CH) domain superfamily of actin cross-linking proteins. Like other members of this superfamily, which include α-actinin, β-spectrin, dystrophin, ABP-120 and filamin, it has a conserved 27 kDa actin-binding domain that contains a tandem duplication of a sequence that is homologous to calponin. In addition to cross-linking actin filaments into bundles and networks, CH domains also bind intermediate filaments and some signal transduction proteins to the actin cytoskeleton. Structural comparison of actin filaments and fimbrin CH domain-decorated actin filaments has revealed changes in the actin structure due to fimbrin-mediated cross-linking that may affect the actin filaments' affinity for other actin-binding proteins and may be part of the regulation of the cytoskeleton itself.^[6]

In humans, three highly homologous, strictly tissue and locale specific isoforms have been identified: I-, T- and L-fimbrin.^[6] L-fimbrin is found in only normal or transformed leukocytes where it becomes phosphorylated in response to other factors such as interleukin-1. I-fimbrin is expressed by intestine and kidney epithelial cells.^[7] T-fimbrin is found in epithelial and mesenchymal cells derived from solid tissue where it does not become phosphorylated. Differences in expression, sequence and phosphorylation among the various fimbrin isoforms suggest the likelihood of functional differences.^[7]

Function

Fimbrin is present in several distinct structures in different cell types, including intestinal microvilli, hair cell stereocilia and fibroblast filopodia.^[7] It is usually associated with polarized actin filaments in membrane ruffles, filopodia, stereocilia and adhesion plaques. Sequence homology and biochemical properties show that fimbrin is highly conserved from yeast to humans. Yeast mutants lacking fimbrin are defective in morphogenesis and endocytosis.^[6]

Owing to the close proximity of its tandem actin-binding domains, fimbrin directs the formation of tightly bundled actin filaments that participate in dynamic processes, including cytokinesis in yeast and host cell invasion by enteropathic bacteria. Although fimbrin's involvement in processes like these as well as its role in assembly and regulation of microfilament networks are well documented, there are fewer experimental data describing the overall domain organization of the molecule. Klein et al. (2004) detailed the crystal structure of the Arabidopsis thaliana and Schizosaccharomyces pombe fimbrin cores in an attempt to highlight the compact and distinctly asymmetric organization of the fimbrin molecule. This structural study of the fimbrin core represents the first detailed structural description of a functional actin cross-linking protein.^[8]

References

Further reading