PLS3

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Plastin 3 (T isoform)
File:PBB Protein PLS3 image.jpg
PDB rendering based on 1aoa.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PLS3 ; T-PLASTIN
External IDs Template:OMIM5 Template:MGI HomoloGene68250
RNA expression pattern
File:PBB GE PLS3 201215 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Plastin 3 (T isoform), also known as PLS3, is a human gene.[1]

Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. In humans, two ubiquitous plastin isoforms (L and T) have been identified. Plastin 1 (otherwise known as Fimbrin) is a third distinct plastin isoform which is specifically expressed at high levels in the small intestine. The L isoform is expressed only in hemopoietic cell lineages, while the T isoform has been found in all other normal cells of solid tissues that have replicative potential (fibroblasts, endothelial cells, epithelial cells, melanocytes, etc.). The C-terminal 570 amino acids of the T-plastin and L-plastin proteins are 83% identical. It contains a potential calcium-binding site near the N terminus.[1]

References

  1. 1.0 1.1 "Entrez Gene: PLS3 plastin 3 (T isoform)".

Further reading

  • Lin CS, Aebersold RH, Leavitt J (1990). "Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain". Mol. Cell. Biol. 10 (4): 1818–21. PMID 2378651.
  • Lin CS, Aebersold RH, Kent SB; et al. (1989). "Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts". Mol. Cell. Biol. 8 (11): 4659–68. PMID 3211125.
  • Goldstein D, Djeu J, Latter G; et al. (1985). "Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes". Cancer Res. 45 (11 Pt 2): 5643–7. PMID 4053036.
  • Arpin M, Friederich E, Algrain M; et al. (1995). "Functional differences between L- and T-plastin isoforms". J. Cell Biol. 127 (6 Pt 2): 1995–2008. PMID 7806577.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Lin CS, Shen W, Chen ZP; et al. (1994). "Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney". Mol. Cell. Biol. 14 (4): 2457–67. PMID 8139549.
  • Lin CS, Park T, Chen ZP, Leavitt J (1993). "Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells". J. Biol. Chem. 268 (4): 2781–92. PMID 8428952.
  • Goldsmith SC, Pokala N, Shen W; et al. (1997). "The structure of an actin-crosslinking domain from human fimbrin". Nat. Struct. Biol. 4 (9): 708–12. PMID 9302997.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Shoeman RL, Hartig R, Hauses C, Traub P (2003). "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease". Cell Biol. Int. 26 (6): 529–39. PMID 12119179.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Rao RM, Rama S, Rao AJ (2004). "Changes in T-plastin expression with human trophoblast differentiation". Reprod. Biomed. Online. 7 (2): 235–42. PMID 14567899.
  • Su MW, Dorocicz I, Dragowska WH; et al. (2004). "Aberrant expression of T-plastin in Sezary cells". Cancer Res. 63 (21): 7122–7. PMID 14612505.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Giganti A, Plastino J, Janji B; et al. (2005). "Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement". J. Cell. Sci. 118 (Pt 6): 1255–65. doi:10.1242/jcs.01698. PMID 15741236.
  • Ralser M, Nonhoff U, Albrecht M; et al. (2005). "Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways". Hum. Mol. Genet. 14 (19): 2893–909. doi:10.1093/hmg/ddi321. PMID 16115810.
  • Ikeda H, Sasaki Y, Kobayashi T; et al. (2006). "The role of T-fimbrin in the response to DNA damage: silencing of T-fimbrin by small interfering RNA sensitizes human liver cancer cells to DNA-damaging agents". Int. J. Oncol. 27 (4): 933–40. PMID 16142308.
  • Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.

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