ACTR1A

ARP1 actin-related protein 1 homolog A, centractin alpha (yeast)
Identifiers
SymbolsACTR1A ; ARP1; CTRN1
External IDsOMIM: 605143 MGI: 1858964 HomoloGene: 21173 GeneCards: ACTR1A Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez1012154130
EnsemblENSG00000138107ENSMUSG00000025228
UniProtP61163P61164
RefSeq (mRNA)NM_005736NM_016860
RefSeq (protein)NP_005727NP_058556
Location (UCSC)Chr 10:
104.24 – 104.26 Mb		Chr 19:
46.38 – 46.4 Mb
PubMed search

Alpha-centractin (yeast) or ARP1 is a protein that in humans is encoded by the ACTR1A gene.[1][2]

Function

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]

Interactions

ACTR1A has been shown to interact with SPTBN2.[13][10]

References

  1. ↑ 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. PMID 1528266.
  2. ↑ 2.0 2.1 "Entrez Gene: ACTR1A ARP1 actin-related protein 1 homolog A, centractin alpha (yeast)".
  3. ↑ Schafer DA, Gill SR, Cooper JA, Heuser JE, Schroer TA (1994). "Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin". The Journal of Cell Biology 126 (2): 403–412. doi:10.1083/jcb.126.2.403. PMC 2200042. PMID 7518465.
  4. ↑ Bingham JB, Schroer TA (1999). "Self-regulated polymerization of the actin-related protein Arp1". Curr. Biol. 9 (4): 223–6. doi:10.1016/S0960-9822(99)80095-5. PMID 10074429.
  5. ↑ 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. doi:10.1073/pnas.92.5.1634. PMC 42574. PMID 7878030.
  6. ↑ 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. PMID 10607597.
  7. ↑ 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. PMID 10671518.
  8. ↑ Eckley DM, Schroer TA (2003). "Interactions between the evolutionarily conserved, actin-related protein, Arp11, actin, and Arp1". Mol. Biol. Cell 14 (7): 2645–54. doi:10.1091/mbc.E03-01-0049. PMC 165665. PMID 12857853.
  9. ↑ Holleran EA, Tokito MK, Karki S, Holzbaur EL (1996). "Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles". J. Cell Biol. 135 (6 Pt 2): 1815–29. doi:10.1083/jcb.135.6.1815. PMC 2133946. PMID 8991093.
  10. ↑ 10.0 10.1 Holleran 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. PMID 11461920.
  11. ↑ 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. PMID 11172722.
  12. ↑ Johansson M, Rocha N, Zwart W, Jordens I, Janssen L, Kuijl C, Olkkonen VM, Neefjes J (2007). "Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin". J. Cell Biol. 176 (4): 459–71. doi:10.1083/jcb.200606077. PMC 2063981. PMID 17283181.
  13. ↑ 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. PMID 11357136.

Further reading

External links