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Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.
The Wiskott–Aldrich Syndrome protein (WASp) is a 502-amino acid protein expressed in cells of the hematopoietic system that in humans is encoded by the WAS gene. In the inactive state, WASp exists in an autoinhibited conformation with sequences near its C-terminus binding to a region near its N-terminus. Its activation is dependent upon CDC42 and PIP2 acting to disrupt this interaction, causing the WASp protein to 'open'. This exposes a domain near the WASp C-terminus that binds to and activates the Arp2/3 complex. Activated Arp2/3 nucleates new F-actin.
Formin-binding protein 1 is a protein that in humans is encoded by the FNBP1 gene.
Profilin-2 is a protein that in humans is encoded by the PFN2 gene.
Protein diaphanous homolog 1 is a protein that in humans is encoded by the DIAPH1 gene.
FH1/FH2 domain-containing protein 1 is a protein that in humans is encoded by the FHOD1 gene.
Protein flightless-1 homolog is a protein that in humans is encoded by the FLII gene.
Anillin is a conserved protein implicated in cytoskeletal dynamics during cellularization and cytokinesis. The ANLN gene in humans and the scraps gene in Drosophila encode Anillin. In 1989, anillin was first isolated in embryos of Drosophila melanogaster. It was identified as an F-actin binding protein. Six years later, the anillin gene was cloned from cDNA originating from a Drosophila ovary. Staining with anti-anillin antibody showed the anillin localizes to the nucleus during interphase and to the contractile ring during cytokinesis. These observations agree with further research that found anillin in high concentrations near the cleavage furrow coinciding with RhoA, a key regulator of contractile ring formation.
MKL/megakaryoblastic leukemia 1 is a protein that in humans is encoded by the MKL1 gene.
Protein diaphanous homolog 2 is a protein that in humans is encoded by the DIAPH2 gene.
Formin-binding protein 1-like is a protein that in humans is encoded by the FNBP1L gene.
60S ribosomal protein L13 is a protein that in humans is encoded by the RPL13 gene.
Actin-related protein 2/3 complex subunit 1A is a protein that in humans is encoded by the ARPC1A gene.
Disheveled-associated activator of morphogenesis 1 is a protein that in humans is encoded by the DAAM1 gene. Evidence of alternative splicing has been observed for this gene but the full-length nature of these variants has not been determined.
WW domain-binding protein 4 is a protein that in humans is encoded by the WBP4 gene.
Protein cordon-bleu is a protein that in humans is encoded by the COBL gene.
mDia1 is a member of the protein family called the formins and is a Rho effector. It is the mouse version of the diaphanous homolog 1 of Drosophila. mDia1 localizes to cells' mitotic spindle and midbody, plays a role in stress fiber and filopodia formation, phagocytosis, activation of serum response factor, formation of adherens junctions, and it can act as a transcription factor. mDia1 accelerates actin nucleation and elongation by interacting with barbed ends of actin filaments. The gene encoding mDia1 is located on Chromosome 18 of Mus musculus and named Diap1.
Inverted formin-2 is a protein that in humans is encoded by the INF2 gene. It belongs to the protein family called the formins. It has two splice isoforms, CAAX which localizes to the endoplasmic reticulum and non-CAAX which localizes to focal adhesions and the cytoplasm with enrichment at the Golgi. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. INF2 accelerates actin nucleation and elongation by interacting with barbed ends of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments.
Arp2/3 complex is a seven-subunit protein complex that plays a major role in the regulation of the actin cytoskeleton. It is a major component of the actin cytoskeleton and is found in most actin cytoskeleton-containing eukaryotic cells. Two of its subunits, the Actin-Related Proteins ARP2 and ARP3, closely resemble the structure of monomeric actin and serve as nucleation sites for new actin filaments. The complex binds to the sides of existing ("mother") filaments and initiates growth of a new ("daughter") filament at a distinctive 70 degree angle from the mother. Branched actin networks are created as a result of this nucleation of new filaments. The regulation of rearrangements of the actin cytoskeleton is important for processes like cell locomotion, phagocytosis, and intracellular motility of lipid vesicles.
An actin nucleation core is a protein trimer with three actin monomers. It is called a nucleation core because it leads to the energetically favorable elongation reaction once a tetramer is formed from a trimer. Actin protein dimers and trimers are energetically unfavorable.Actin nucleators like the Arp2/3 complex of proteins from the formin family are most frequently involved in this process. Actin nucleation factors start the polymerization of actin within cells.
References
- ↑ "SPIRE1 - Protein spire homolog 1 - Homo sapiens (Human) - SPIRE1 gene & protein". www.uniprot.org.
- ↑ Manseau, L. J.; Schüpbach, T. (September 19, 1989). "cappuccino and spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo". Genes & Development. 3 (9): 1437–1452. doi: 10.1101/gad.3.9.1437 . PMID 2514120.
- ↑ Quinlan, Margot E.; Heuser, John E.; Kerkhoff, Eugen; Mullins, R. Dyche (2005-01-27). "Drosophila Spire is an actin nucleation factor". Nature. 433 (7024): 382–388. Bibcode:2005Natur.433..382Q. doi:10.1038/nature03241. ISSN 1476-4687. PMID 15674283. S2CID 4424757.
- ↑ Vizcarra, Christina L.; Kreutz, Barry; Rodal, Avital A.; Toms, Angela V.; Lu, Jun; Zheng, Wei; Quinlan, Margot E.; Eck, Michael J. (2011-07-19). "Structure and function of the interacting domains of Spire and Fmn-family formins". Proceedings of the National Academy of Sciences. 108 (29): 11884–11889. Bibcode:2011PNAS..10811884V. doi: 10.1073/pnas.1105703108 . PMC 3141961 . PMID 21730168.
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