| 释义 |
- Function
- Clinical significance
- References
- Further reading
{{Infobox_gene}}Plastin-3 is a highly conserved protein that in humans is encoded by the PLS3 gene on the X chromosome.[1][2] 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.[2] Clinical significance Defects in PLS3 are associated with osteoporosis and bone fracture in humans and in knockout zebrafish.[3] References1. ^{{cite journal | vauthors = 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 |date=Mar 1993 | pmid = 8428952 | pmc = | doi = }}
2. ^1 {{cite web | title = Entrez Gene: PLS3 plastin 3 (T isoform)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5358| accessdate = }}
3. ^{{cite journal | vauthors = van Dijk FS, Zillikens MC, Micha D, Riessland M, Marcelis CL, de Die-Smulders CE, Milbradt J, Franken AA, Harsevoort AJ, Lichtenbelt KD| title = PLS3 Mutations in X-Linked Osteoporosis with Fractures | journal = N. Engl. J. Med. | volume = 369| issue = 16| pages = 1529–36|date=October 2013 | pmid = 24088043 | doi = 10.1056/NEJMoa1308223 |display-authors=etal| citeseerx = 10.1.1.713.901 }}
Further reading{{refbegin | 2}}- {{cite journal | vauthors=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= 10.1128/MCB.10.4.1818| pmc=362293 }}
- {{cite journal |vauthors=Lin CS, Aebersold RH, Kent SB, etal |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= 1988 |pmid= 3211125 |doi= 10.1128/MCB.8.11.4659| pmc=365555 }}
- {{cite journal |vauthors=Goldstein D, Djeu J, Latter G, etal |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 |vauthors=Arpin M, Friederich E, Algrain M, etal |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=10.1083/jcb.127.6.1995 | pmc=2120298 }}
- {{cite journal | vauthors=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=10.1016/0378-1119(94)90802-8 }}
- {{cite journal |vauthors=Lin CS, Shen W, Chen ZP, etal |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= 10.1128/mcb.14.4.2457| pmc=358613 }}
- {{cite journal |vauthors=Goldsmith SC, Pokala N, Shen W, etal |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=10.1038/nsb0997-708 }}
- {{cite journal | vauthors=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=10.1006/cbir.2002.0895 }}
- {{cite journal | vauthors=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=10.1016/S1472-6483(10)61758-0 }}
- {{cite journal |vauthors=Su MW, Dorocicz I, Dragowska WH, etal |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 |vauthors=Giganti A, Plastino J, Janji B, etal |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 |vauthors=Ralser M, Nonhoff U, Albrecht M, etal |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 |vauthors=Ikeda H, Sasaki Y, Kobayashi T, etal |title=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 |journal=Int. J. Oncol. |volume=27 |issue= 4 |pages= 933–40 |year= 2006 |pmid= 16142308 |doi= 10.3892/ijo.27.4.933}}
{{refend}}{{PDB Gallery|geneid=5358}}{{gene-X-stub}} 1 : EF-hand-containing proteins |