ACTR1B: Difference between revisions
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| summary_text = This gene encodes a 42.3 kD subunit of dynactin, a macromolecular complex consisting of 10 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit, like ACTR1A, is an actin-related protein. These two proteins are of equal length and share 90% amino acid identity. They are present in a constant ratio of approximately 1:15 in the dynactin complex.<ref name="entrez">{{cite web | title = Entrez Gene: ACTR1B ARP1 actin-related protein 1 homolog B, centractin beta (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10120| accessdate = }}</ref> | | summary_text = This gene encodes a 42.3 kD subunit of dynactin, a macromolecular complex consisting of 10 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit, like ACTR1A, is an actin-related protein. These two proteins are of equal length and share 90% amino acid identity. They are present in a constant ratio of approximately 1:15 in the dynactin complex.<ref name="entrez">{{cite web | title = Entrez Gene: ACTR1B ARP1 actin-related protein 1 homolog B, centractin beta (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10120| accessdate = }}</ref> | ||
}} | }} | ||
==References== | |||
{{reflist}} | |||
==Further reading== | |||
{{refbegin | 2}} | |||
{{PBB_Further_reading | |||
| citations = | |||
*{{cite journal | author=Clark SW, Meyer DI |title=Centractin is an actin homologue associated with the centrosome. |journal=Nature |volume=359 |issue= 6392 |pages= 246-50 |year= 1992 |pmid= 1356230 |doi= 10.1038/359246a0 }} | |||
*{{cite journal | author=Lees-Miller JP, Helfman DM, Schroer TA |title=A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. |journal=Nature |volume=359 |issue= 6392 |pages= 244-6 |year= 1992 |pmid= 1528266 |doi= 10.1038/359244a0 }} | |||
*{{cite journal | author=Schafer DA, Gill SR, Cooper JA, ''et al.'' |title=Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. |journal=J. Cell Biol. |volume=126 |issue= 2 |pages= 403-12 |year= 1994 |pmid= 7518465 |doi= }} | |||
*{{cite journal | author=Clark SW, Staub O, Clark IB, ''et al.'' |title=Beta-centractin: characterization and distribution of a new member of the centractin family of actin-related proteins. |journal=Mol. Biol. Cell |volume=5 |issue= 12 |pages= 1301-10 |year= 1995 |pmid= 7696711 |doi= }} | |||
*{{cite journal | author=Waterman-Storer CM, Karki S, Holzbaur EL |title=The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 5 |pages= 1634-8 |year= 1995 |pmid= 7878030 |doi= }} | |||
*{{cite journal | author=Holleran EA, Tokito MK, Karki S, Holzbaur EL |title=Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. |journal=J. Cell Biol. |volume=135 |issue= 6 Pt 2 |pages= 1815-29 |year= 1997 |pmid= 8991093 |doi= }} | |||
*{{cite journal | author=Faulkner NE, Vig B, Echeverri CJ, ''et al.'' |title=Localization of motor-related proteins and associated complexes to active, but not inactive, centromeres. |journal=Hum. Mol. Genet. |volume=7 |issue= 4 |pages= 671-7 |year= 1998 |pmid= 9499420 |doi= }} | |||
*{{cite journal | author=Bingham JB, Schroer TA |title=Self-regulated polymerization of the actin-related protein Arp1. |journal=Curr. Biol. |volume=9 |issue= 4 |pages= 223-6 |year= 1999 |pmid= 10074429 |doi= }} | |||
*{{cite journal | author=Heimann K, Percival JM, Weinberger R, ''et al.'' |title=Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles. |journal=J. Biol. Chem. |volume=274 |issue= 16 |pages= 10743-50 |year= 1999 |pmid= 10196146 |doi= }} | |||
*{{cite journal | author=Saffery R, Irvine DV, Griffiths B, ''et al.'' |title=Human centromeres and neocentromeres show identical distribution patterns of >20 functionally important kinetochore-associated proteins. |journal=Hum. Mol. Genet. |volume=9 |issue= 2 |pages= 175-85 |year= 2000 |pmid= 10607828 |doi= }} | |||
*{{cite journal | author=Fouquet J, Kann M, Souès S, Melki R |title=ARP1 in Golgi organisation and attachment of manchette microtubules to the nucleus during mammalian spermatogenesis. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue= |pages= 877-86 |year= 2000 |pmid= 10671377 |doi= }} | |||
*{{cite journal | author=Karki S, Tokito MK, Holzbaur EL |title=A dynactin subunit with a highly conserved cysteine-rich motif interacts directly with Arp1. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 4834-9 |year= 2000 |pmid= 10671518 |doi= }} | |||
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }} | |||
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }} | |||
*{{cite journal | author=Holleran EA, Ligon LA, Tokito M, ''et al.'' |title=beta III spectrin binds to the Arp1 subunit of dynactin. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36598-605 |year= 2001 |pmid= 11461920 |doi= 10.1074/jbc.M104838200 }} | |||
*{{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=Carew JA, Jackson AA, Bauer KA |title=ARP1 interacts with the 5' flanking region of the coagulation factor VII gene. |journal=J. Thromb. Haemost. |volume=1 |issue= 6 |pages= 1220-7 |year= 2004 |pmid= 12871323 |doi= }} | |||
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }} | |||
}} | |||
{{refend}} | |||
{{protein-stub}} | |||
{{WikiDoc Sources}} |
Revision as of 21:36, 3 March 2009
ARP1 actin-related protein 1 homolog B, centractin beta (yeast) | |||||||||||
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Identifiers | |||||||||||
Symbols | ACTR1B ; ARP1 | ||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 101541 | ||||||||||
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Orthologs | |||||||||||
Template:GNF Ortholog box | |||||||||||
Species | Human | Mouse | |||||||||
Entrez | n/a | n/a | |||||||||
Ensembl | n/a | n/a | |||||||||
UniProt | n/a | n/a | |||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||
RefSeq (protein) | n/a | n/a | |||||||||
Location (UCSC) | n/a | n/a | |||||||||
PubMed search | n/a | n/a |
ARP1 actin-related protein 1 homolog B, centractin beta (yeast), also known as ACTR1B, is a human gene.[1]
This gene encodes a 42.3 kD subunit of dynactin, a macromolecular complex consisting of 10 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit, like ACTR1A, is an actin-related protein. These two proteins are of equal length and share 90% amino acid identity. They are present in a constant ratio of approximately 1:15 in the dynactin complex.[1]
References
Further reading
- Clark SW, Meyer DI (1992). "Centractin is an actin homologue associated with the centrosome". Nature. 359 (6392): 246–50. doi:10.1038/359246a0. PMID 1356230.
- Lees-Miller JP, Helfman DM, Schroer TA (1992). "A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility". Nature. 359 (6392): 244–6. doi:10.1038/359244a0. PMID 1528266.
- Schafer DA, Gill SR, Cooper JA; et al. (1994). "Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin". J. Cell Biol. 126 (2): 403–12. PMID 7518465.
- Clark SW, Staub O, Clark IB; et al. (1995). "Beta-centractin: characterization and distribution of a new member of the centractin family of actin-related proteins". Mol. Biol. Cell. 5 (12): 1301–10. PMID 7696711.
- Waterman-Storer CM, Karki S, Holzbaur EL (1995). "The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)". Proc. Natl. Acad. Sci. U.S.A. 92 (5): 1634–8. PMID 7878030.
- Holleran EA, Tokito MK, Karki S, Holzbaur EL (1997). "Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles". J. Cell Biol. 135 (6 Pt 2): 1815–29. PMID 8991093.
- Faulkner NE, Vig B, Echeverri CJ; et al. (1998). "Localization of motor-related proteins and associated complexes to active, but not inactive, centromeres". Hum. Mol. Genet. 7 (4): 671–7. PMID 9499420.
- Bingham JB, Schroer TA (1999). "Self-regulated polymerization of the actin-related protein Arp1". Curr. Biol. 9 (4): 223–6. PMID 10074429.
- Heimann K, Percival JM, Weinberger R; et al. (1999). "Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles". J. Biol. Chem. 274 (16): 10743–50. PMID 10196146.
- Saffery R, Irvine DV, Griffiths B; et al. (2000). "Human centromeres and neocentromeres show identical distribution patterns of >20 functionally important kinetochore-associated proteins". Hum. Mol. Genet. 9 (2): 175–85. PMID 10607828.
- Fouquet J, Kann M, Souès S, Melki R (2000). "ARP1 in Golgi organisation and attachment of manchette microtubules to the nucleus during mammalian spermatogenesis". J. Cell. Sci. 113 ( Pt 5): 877–86. PMID 10671377.
- Karki S, Tokito MK, Holzbaur EL (2000). "A dynactin subunit with a highly conserved cysteine-rich motif interacts directly with Arp1". J. Biol. Chem. 275 (7): 4834–9. PMID 10671518.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. PMID 11076863.
- Simpson JC, Wellenreuther R, Poustka A; et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614.
- Holleran EA, Ligon LA, Tokito M; et al. (2001). "beta III spectrin binds to the Arp1 subunit of dynactin". J. Biol. Chem. 276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID 11461920.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Carew JA, Jackson AA, Bauer KA (2004). "ARP1 interacts with the 5' flanking region of the coagulation factor VII gene". J. Thromb. Haemost. 1 (6): 1220–7. PMID 12871323.
- Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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