Plastin-3 is a highly conserved protein that in humans is encoded by the PLS3 gene on the X chromosome.[5][6]

PLS3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPLS3, BMND18, T-plastin, plastin 3
External IDsOMIM: 300131; MGI: 104807; HomoloGene: 128200; GeneCards: PLS3; OMA:PLS3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001136025
NM_001172335
NM_001282337
NM_001282338
NM_005032

NM_001166453
NM_001166454
NM_145629
NM_001346519
NM_001346520

RefSeq (protein)

NP_001129497
NP_001165806
NP_001269266
NP_001269267
NP_005023

NP_001159925
NP_001159926
NP_001333448
NP_001333449
NP_663604

Location (UCSC)Chr X: 115.56 – 115.65 MbChr X: 74.83 – 74.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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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.[6]

Clinical significance

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Defects in PLS3 are associated with osteoporosis and bone fracture in humans and in knockout zebrafish.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000102024Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016382Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lin CS, Park T, Chen ZP, Leavitt J (Mar 1993). "Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells". J Biol Chem. 268 (4): 2781–92. doi:10.1016/S0021-9258(18)53842-4. PMID 8428952.2781-92&rft.date=1993-03&rft_id=info:doi/10.1016/S0021-9258(18)53842-4&rft_id=info:pmid/8428952&rft.aulast=Lin&rft.aufirst=CS&rft.au=Park, T&rft.au=Chen, ZP&rft.au=Leavitt, J&rft_id=https://doi.org/10.1016%2FS0021-9258%2818%2953842-4&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  6. ^ a b "Entrez Gene: PLS3 plastin 3 (T isoform)".
  7. ^ van Dijk FS, Zillikens MC, Micha D, Riessland M, Marcelis CL, de Die-Smulders CE, Milbradt J, Franken AA, Harsevoort AJ, Lichtenbelt KD, et al. (October 2013). "PLS3 Mutations in X-Linked Osteoporosis with Fractures". N. Engl. J. Med. 369 (16): 1529–36. CiteSeerX 10.1.1.713.901. doi:10.1056/NEJMoa1308223. PMID 24088043.1529-36&rft.date=2013-10&rft_id=https://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.713.901#id-name=CiteSeerX&rft_id=info:pmid/24088043&rft_id=info:doi/10.1056/NEJMoa1308223&rft.aulast=van Dijk&rft.aufirst=FS&rft.au=Zillikens, MC&rft.au=Micha, D&rft.au=Riessland, M&rft.au=Marcelis, CL&rft.au=de Die-Smulders, CE&rft.au=Milbradt, J&rft.au=Franken, AA&rft.au=Harsevoort, AJ&rft.au=Lichtenbelt, KD&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">

Further reading

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  • 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. doi:10.1128/MCB.10.4.1818. PMC 362293. PMID 2378651.1818-21&rft.date=1990&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362293#id-name=PMC&rft_id=info:pmid/2378651&rft_id=info:doi/10.1128/MCB.10.4.1818&rft.aulast=Lin&rft.aufirst=CS&rft.au=Aebersold, RH&rft.au=Leavitt, J&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362293&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • Lin CS, Aebersold RH, Kent SB, et al. (1988). "Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts". Mol. Cell. Biol. 8 (11): 4659–68. doi:10.1128/MCB.8.11.4659. PMC 365555. PMID 3211125.4659-68&rft.date=1988&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC365555#id-name=PMC&rft_id=info:pmid/3211125&rft_id=info:doi/10.1128/MCB.8.11.4659&rft.aulast=Lin&rft.aufirst=CS&rft.au=Aebersold, RH&rft.au=Kent, SB&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC365555&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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 4053036.5643-7&rft.date=1985&rft_id=info:pmid/4053036&rft.aulast=Goldstein&rft.aufirst=D&rft.au=Djeu, J&rft.au=Latter, G&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. doi:10.1083/jcb.127.6.1995. PMC 2120298. PMID 7806577.1995-2008&rft.date=1995&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120298#id-name=PMC&rft_id=info:pmid/7806577&rft_id=info:doi/10.1083/jcb.127.6.1995&rft.aulast=Arpin&rft.aufirst=M&rft.au=Friederich, E&rft.au=Algrain, M&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120298&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.1–2&rft.pages=171-4&rft.date=1994&rft_id=info:doi/10.1016/0378-1119(94)90802-8&rft_id=info:pmid/8125298&rft.aulast=Maruyama&rft.aufirst=K&rft.au=Sugano, S&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. doi:10.1128/mcb.14.4.2457. PMC 358613. PMID 8139549.2457-67&rft.date=1994&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC358613#id-name=PMC&rft_id=info:pmid/8139549&rft_id=info:doi/10.1128/mcb.14.4.2457&rft.aulast=Lin&rft.aufirst=CS&rft.au=Shen, W&rft.au=Chen, ZP&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC358613&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. doi:10.1038/nsb0997-708. PMID 9302997. S2CID 9506514.708-12&rft.date=1997&rft_id=https://api.semanticscholar.org/CorpusID:9506514#id-name=S2CID&rft_id=info:pmid/9302997&rft_id=info:doi/10.1038/nsb0997-708&rft.aulast=Goldsmith&rft.aufirst=SC&rft.au=Pokala, N&rft.au=Shen, W&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. doi:10.1006/cbir.2002.0895. PMID 12119179. S2CID 39778155.529-39&rft.date=2003&rft_id=https://api.semanticscholar.org/CorpusID:39778155#id-name=S2CID&rft_id=info:pmid/12119179&rft_id=info:doi/10.1006/cbir.2002.0895&rft.aulast=Shoeman&rft.aufirst=RL&rft.au=Hartig, R&rft.au=Hauses, C&rft.au=Traub, P&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • Rao RM, Rama S, Rao AJ (2004). "Changes in T-plastin expression with human trophoblast differentiation". Reprod. Biomed. Online. 7 (2): 235–42. doi:10.1016/S1472-6483(10)61758-0. PMID 14567899.235-42&rft.date=2004&rft_id=info:doi/10.1016/S1472-6483(10)61758-0&rft_id=info:pmid/14567899&rft.aulast=Rao&rft.aufirst=RM&rft.au=Rama, S&rft.au=Rao, AJ&rft_id=https://doi.org/10.1016%2FS1472-6483%2810%2961758-0&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • Su MW, Dorocicz I, Dragowska WH, et al. (2004). "Aberrant expression of T-plastin in Sezary cells". Cancer Res. 63 (21): 7122–7. PMID 14612505.7122-7&rft.date=2004&rft_id=info:pmid/14612505&rft.aulast=Su&rft.aufirst=MW&rft.au=Dorocicz, I&rft.au=Dragowska, WH&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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 15741236.1255-65&rft.date=2005&rft_id=info:doi/10.1242/jcs.01698&rft_id=info:pmid/15741236&rft.aulast=Giganti&rft.aufirst=A&rft.au=Plastino, J&rft.au=Janji, B&rft_id=https://doi.org/10.1242%2Fjcs.01698&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. hdl:11858/00-001M-0000-0010-85BB-5. PMID 16115810.2893-909&rft.date=2005&rft_id=info:hdl/11858/00-001M-0000-0010-85BB-5&rft_id=info:pmid/16115810&rft_id=info:doi/10.1093/hmg/ddi321&rft.aulast=Ralser&rft.aufirst=M&rft.au=Nonhoff, U&rft.au=Albrecht, M&rft_id=https://doi.org/10.1093%2Fhmg%2Fddi321&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">
  • 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. doi:10.3892/ijo.27.4.933. PMID 16142308.933-40&rft.date=2006&rft_id=info:doi/10.3892/ijo.27.4.933&rft_id=info:pmid/16142308&rft.aulast=Ikeda&rft.aufirst=H&rft.au=Sasaki, Y&rft.au=Kobayashi, T&rfr_id=info:sid/en.wikipedia.org:PLS3" class="Z3988">