PLS3

PLS3

Plastin 3 (T isoform), also known as PLS3, is a human gene.cite web | title = Entrez Gene: PLS3 plastin 3 (T isoform)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5358| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PLS3 plastin 3 (T isoform)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5358| accessdate = ]

References

Further reading

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

*cite journal | author=Ewing RM, Chu P, Elisma F, "et al." |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134

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