Biology:PLS3

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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

Function

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.

Clinical significance

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

Further reading

• "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. 1990. doi:10.1128/MCB.10.4.1818. PMID 2378651. 
• "Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts". Mol. Cell. Biol. 8 (11): 4659–68. 1988. doi:10.1128/MCB.8.11.4659. PMID 3211125. 
• "Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes". Cancer Res. 45 (11 Pt 2): 5643–7. 1985. PMID 4053036. 
• "Functional differences between L- and T-plastin isoforms". J. Cell Biol. 127 (6 Pt 2): 1995–2008. 1995. doi:10.1083/jcb.127.6.1995. PMID 7806577. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney". Mol. Cell. Biol. 14 (4): 2457–67. 1994. doi:10.1128/mcb.14.4.2457. PMID 8139549. 
• "The structure of an actin-crosslinking domain from human fimbrin". Nat. Struct. Biol. 4 (9): 708–12. 1997. doi:10.1038/nsb0997-708. PMID 9302997. 
• "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease". Cell Biol. Int. 26 (6): 529–39. 2003. doi:10.1006/cbir.2002.0895. PMID 12119179. 
• "Changes in T-plastin expression with human trophoblast differentiation". Reprod. Biomed. Online 7 (2): 235–42. 2004. doi:10.1016/S1472-6483(10)61758-0. PMID 14567899. 
• "Aberrant expression of T-plastin in Sezary cells". Cancer Res. 63 (21): 7122–7. 2004. PMID 14612505. 
• "Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement". J. Cell Sci. 118 (Pt 6): 1255–65. 2005. doi:10.1242/jcs.01698. PMID 15741236. 
• "Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways". Hum. Mol. Genet. 14 (19): 2893–909. 2005. doi:10.1093/hmg/ddi321. PMID 16115810. 
• "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. 2006. doi:10.3892/ijo.27.4.933. PMID 16142308.