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== Clinical significance == | == Clinical significance == | ||
Defects in PLS3 are associated with [[osteoporosis]] and bone fracture in humans and in [[gene knockout|knockout]] zebrafish.<ref name="pmid24088043">{{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}}</ref> | Defects in PLS3 are associated with [[osteoporosis]] and bone fracture in humans and in [[gene knockout|knockout]] zebrafish.<ref name="pmid24088043">{{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 }}</ref> | ||
==References== | ==References== | ||
| Line 15: | Line 15: | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{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 | *{{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= | 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 | *{{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= | 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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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 | *{{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}} | {{refend}} | ||
Latest revision as of 05:09, 8 September 2018
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| Location (UCSC) | n/a | n/a | |||||
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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]
References
- ↑ 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. PMID 8428952.
- ↑ 2.0 2.1 "Entrez Gene: PLS3 plastin 3 (T isoform)".
- ↑ 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.
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. PMC 362293. PMID 2378651.
- 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. PMC 365555. 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. doi:10.1083/jcb.127.6.1995. PMC 2120298. 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1128/mcb.14.4.2457. PMC 358613. PMID 8139549.
- 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.
- 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.
- 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.
- 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.
- 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. doi:10.3892/ijo.27.4.933. PMID 16142308.
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