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Gene Review

CYIIA  -  actin

Strongylocentrotus purpuratus

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Disease relevance of LOC373188

  • The remarkable degree of conservation of the actin protein is reflected in concomitant conservation of the protein-coding nucleotide sequences of the messenger RNA, which has allowed the use of a cDNA probe to isolate actin sequences from a human phage library [1].

High impact information on LOC373188

  • Spatially deranged though temporally correct expression of Strongylocentrotus purpuratus actin gene fusion in transgenic embryos of a different sea urchin family [2].
  • Using four-dimensional microscopy and a probe for active RhoA, we show that active RhoA concentrates in a precisely bounded zone before cytokinesis and is independent of actin assembly [3].
  • Energy transfer and sedimentation experiments indicate a net disassembly of actin filaments and an increase in the steady-state nonfilamentous actin concentration in the presence of Ca2+ ions and the 45,000-mol-wt protein [4].
  • Sea urchin tube feet: unique structures that allow a cytological and molecular approach to the study of actin and its gene expression [1].
  • In a cell-free system from rabbit reticulocytes, total RNA from tube feet stimulated the synthesis of one protein that represented 80% of the total methionine incorporation, migrated with the properties characteristic of actin in a two-dimensional gel system, and on proteolysis yielded fragments identical to purified rabbit actin [1].

Biological context of LOC373188

  • There are at least five distinct types of sea urchin actin gene, some of which are represented by multiple copies in the genome [5].
  • The actin gene types are distinguished by nonhomologous flanking sequences and intervening sequences, though the protein coding sequences appear in most cases to be quite similar [5].
  • Different repetitive sequences were located to either side of most of the actin genes, and in most observed cases the repeat sequences which were adjacent to actin genes of a given type were similar [5].
  • The repeat sequences flanking the actin genes belonged to families which were transcribed, but those repeats in the neighborhood of the actin genes which have been investigated were not themselves represented in the stable RNAs of eggs or early embryos [5].
  • Cytokinesis in animal cells results from the assembly and constriction of a circumferential array of actin filaments and myosin-2 [3].

Anatomical context of LOC373188

  • Actin is the major protein of both forms of the cytoskeleton [6].
  • Ultrastructurally, the formation of the filopodia results from a progressive reorganization of actin-containing filaments into bundles that are radially oriented [7].
  • Posttranscriptional regulation was not observed for the SM50 gene whose mRNA accumulates only in primary mesenchyme cells, or for actin CyI which is expressed predominantly in E/M cells of gastrulae [8].
  • The CyIIIa cytoskeletal actin gene of Strongylocentrotus purpuratus is expressed specifically in the aboral ectoderm [9].
  • We confirm prior observations that the prevalence of actin mRNA in the unfertilized egg is low [10].

Associations of LOC373188 with chemical compounds


Other interactions of LOC373188

  • The CyIIIa cytoskeletal actin gene of the sea urchin Strongylocentrotus purpuratus is activated in late cleavage and expressed exclusively in the aboral ectoderm territory of the embryo [16].
  • The general organization and primary amino acid sequences of the S. purpuratus cytoskeletal actin genes CyIIb and CyIIIb have been determined from restriction enzyme analysis, DNA sequencing, and RNA mapping studies [17].
  • Comparison of the protein-coding sequence of this muscle actin gene (pSpG28) with that of two linked sea urchin cytoskeletal actin genes (pSpG17 and CyIIa) reveals a region of exceptional sequence conservation from codon 61 through codon 120 [18].

Analytical, diagnostic and therapeutic context of LOC373188

  • Two-dimensional gel electrophoresis resolved two, and possible three, species of actin for each sea urchin of which the dominant component was analogous to the beta form in vertebrates [1].
  • As analyzed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), the pelleted spindles contain 18% tubulin, variable amounts of actin (2-8%), and an unidentified protein of 55 kdaltons in a constant weight ratio to tubulin (1:2.5) [19].
  • In one such case, that of actin CyIIa, which is normally restricted to mesenchyme cells, in situ hybridization demonstrates that the fraction of dissociated cells expressing this message is 4- to 5-fold higher than in the normal embryo [20].
  • The measurements were obtained by probe excess titrations of these RNAs, using a set of single-stranded RNA probes each identifying the mRNA transcripts of a specific actin gene [10].
  • Both the plasma membrane and cortical vesicle membrane samples were found by immunoblotting to contain actin [21].


  1. Sea urchin tube feet: unique structures that allow a cytological and molecular approach to the study of actin and its gene expression. Kabat-Zinn, J., Singer, R.H. J. Cell Biol. (1981) [Pubmed]
  2. Spatially deranged though temporally correct expression of Strongylocentrotus purpuratus actin gene fusion in transgenic embryos of a different sea urchin family. Franks, R.R., Hough-Evans, B.R., Britten, R.J., Davidson, E.H. Genes Dev. (1988) [Pubmed]
  3. A microtubule-dependent zone of active RhoA during cleavage plane specification. Bement, W.M., Benink, H.A., von Dassow, G. J. Cell Biol. (2005) [Pubmed]
  4. A 45,000-mol-wt protein from unfertilized sea urchin eggs severs actin filaments in a calcium-dependent manner and increases the steady-state concentration of nonfilamentous actin. Wang, L.L., Spudich, J.A. J. Cell Biol. (1984) [Pubmed]
  5. Organization and expression of multiple actin genes in the sea urchin. Scheller, R.H., McAllister, L.B., Crain, W.R., Durica, D.S., Posakony, J.W., Thomas, T.L., Britten, R.J., Davidson, E.H. Mol. Cell. Biol. (1981) [Pubmed]
  6. Isolation and characterization of two forms of a cytoskeleton. Edds, K.T. J. Cell Biol. (1979) [Pubmed]
  7. Dynamic aspects of filopodial formation by reorganization of microfilaments. Edds, K.T. J. Cell Biol. (1977) [Pubmed]
  8. Posttranscriptional regulation of ectoderm-specific gene expression in early sea urchin embryos. Gagnon, M.L., Angerer, L.M., Angerer, R.C. Development (1992) [Pubmed]
  9. Spatial and temporal information processing in the sea urchin embryo: modular and intramodular organization of the CyIIIa gene cis-regulatory system. Kirchhamer, C.V., Davidson, E.H. Development (1996) [Pubmed]
  10. Activation of sea urchin actin genes during embryogenesis. Measurement of transcript accumulation from five different genes in Strongylocentrotus purpuratus. Lee, J.J., Calzone, F.J., Britten, R.J., Angerer, R.C., Davidson, E.H. J. Mol. Biol. (1986) [Pubmed]
  11. SpCOUP-TF: a sea urchin member of the steroid/thyroid hormone receptor family. Chan, S.M., Xu, N., Niemeyer, C.C., Bone, J.R., Flytzanis, C.N. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  12. Tubulin polymerization in unfertilized sea-urchin eggs induced by elevated temperature. Harris, P.J., Clason, E.L., Prier, K.R. J. Cell. Sci. (1989) [Pubmed]
  13. The chromosomal arrangement of two linked actin genes in the sea urchin S. purpuratus. Schuler, M.A., Keller, E.B. Nucleic Acids Res. (1981) [Pubmed]
  14. Measurements of mechanical properties of the blastula wall reveal which hypothesized mechanisms of primary invagination are physically plausible in the sea urchin Strongylocentrotus purpuratus. Davidson, L.A., Oster, G.F., Keller, R.E., Koehl, M.A. Dev. Biol. (1999) [Pubmed]
  15. The 50 kDa protein-actin complex from unfertilized sea-urchin (Strongylocentrotus purpuratus) eggs. Interaction with actin. Golsteyn, R.M., Waisman, D.M. Biochem. J. (1989) [Pubmed]
  16. SpZ12-1, a negative regulator required for spatial control of the territory-specific CyIIIa gene in the sea urchin embryo. Wang, D.G., Kirchhamer, C.V., Britten, R.J., Davidson, E.H. Development (1995) [Pubmed]
  17. DNA sequence analysis and structural relationships among the cytoskeletal actin genes of the sea urchin Strongylocentrotus purpuratus. Durica, D.S., Garza, D., Restrepo, M.A., Hryniewicz, M.M. J. Mol. Evol. (1988) [Pubmed]
  18. The sequence of a sea urchin muscle actin gene suggests a gene conversion with a cytoskeletal actin gene. Crain, W.R., Boshar, M.F., Cooper, A.D., Durica, D.S., Nagy, A., Steffen, D. J. Mol. Evol. (1987) [Pubmed]
  19. Dynein-like Mg2+-ATPase in mitotic spindles isolated from sea urchin embryos (Strongylocentrotus droebachiensis). Pratt, M.M., Otter, T., Salmon, E.D. J. Cell Biol. (1980) [Pubmed]
  20. Altered expression of spatially regulated embryonic genes in the progeny of separated sea urchin blastomeres. Hurley, D.L., Angerer, L.M., Angerer, R.C. Development (1989) [Pubmed]
  21. Purification and characterization of a cortical secretory vesicle membrane fraction. Vater, C.A., Jackson, R.C. Dev. Biol. (1989) [Pubmed]
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