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This gene encodes a 42.6 kD subunit of dynactin, a macromolecular complex consisting of 10-11 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 is present in 8-13 copies per dynactin molecule, and is the most abundant molecule in the dynactin complex. It is an actin-related protein, and is approximately 60% identical at the amino acid level to conventional actin.[2] ARP1 forms a 37 nm filament-like structure and is the core of the dynactin complex.[3] It only exists in the dynactin complex in vivo. Highly purified, native Arp1 polymerize rapidly at extremely low concentrations into short filaments in vitro that were similar, but not identical, in length to those in dynactin. With time, these Arp1 filaments appeared to anneal to form longer assemblies but never attained the length of conventional actin filaments. As for conventional actin, Arp1 can bind and hydrolyze ATP, and Arp1 assembly is accompanied by nucleotide hydrolysis.[4]
It has been reported that Arp1 interacts with other dynactin components including DCTN1/p150Glued,[5]DCTN4/p62[6][7] and Actr10/Arp11.[8] Arp1 has been shown as the domain for dynactin binding to membrane vesicles (such as Golgi or late endosome) through its association with β-spectrin.[9][10][11][12]
↑Lees-Miller JP, Helfman DM, Schroer TA (Oct 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. PMID1528266.
↑Garces JA, Clark IB, Meyer DI, Vallee RB (1999). "Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin cytoskeleton". Curr. Biol. 9 (24): 1497–500. doi:10.1016/S0960-9822(00)80122-0. PMID10607597.
↑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. doi:10.1074/jbc.275.7.4834. PMID10671518.
↑ 10.010.1Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (2001). "beta III spectrin binds to the Arp1 subunit of dynactin". J. Biol. Chem. 276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID11461920.
↑Muresan V, Stankewich MC, Steffen W, Morrow JS, Holzbaur EL, Schnapp BJ (2001). "Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: a role for spectrin and acidic phospholipids". Mol. Cell. 7 (1): 173–83. doi:10.1016/S1097-2765(01)00165-4. PMID11172722.
↑Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A, Niehrs C (2001). "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins". Nature. 411 (6835): 321–5. doi:10.1038/35077108. PMID11357136.
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. PMID1356230.
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. doi:10.1093/hmg/7.4.671. PMID9499420.
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. doi:10.1074/jbc.274.16.10743. PMID10196146.
Clark IB, Meyer DI (2000). "Overexpression of normal and mutant Arp1alpha (centractin) differentially affects microtubule organization during mitosis and interphase". J. Cell Sci. 112 (20): 3507–18. PMID10504299.
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. doi:10.1093/hmg/9.2.175. PMID10607828.
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 (5): 877–86. PMID10671377.
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. doi:10.1046/j.1538-7836.2003.00227.x. PMID12871323.