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Gene Review

PPP1R9A  -  protein phosphatase 1, regulatory subunit 9A

Homo sapiens

Synonyms: FLJ20068, KIAA1222, NRB1, NRBI, Neurabin-1, ...
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High impact information on PPP1R9A

  • Neurabin was also concentrated in the lamellipodia of the growth cone during the development of neurons [1].
  • Neurabin: a novel neural tissue-specific actin filament-binding protein involved in neurite formation [1].
  • We moreover cloned the cDNA of neurabin from a rat brain cDNA library and characterized native and recombinant proteins [1].
  • Targeting protein phosphatase 1 (PP1) to the actin cytoskeleton: the neurabin I/PP1 complex regulates cell morphology [2].
  • In vitro and in vivo studies suggested that the actin-binding domain attenuated protein kinase A (PKA) phosphorylation of neurabin I [2].

Biological context of PPP1R9A


Anatomical context of PPP1R9A

  • Biochemical and cellular studies showed that an N-terminal F-actin-binding domain dictated neurabin I localization at actin cytoskeleton and promoted disassembly of stress fibers [2].
  • Mutation of the PP1-binding motif or PP1 inhibition by okadaic acid and calyculin A abolished filopodia and restored stress fibers in cells expressing neurabin I [2].
  • TGN38 and neurabin also interact in vivo as demonstrated by coimmunoprecipitation from stably transfected PC12 cells [3].
  • In addition, they impaired the ability of PP1 to bind neurabin-I, the neuronal regulatory subunit, and G(M), the skeletal muscle glycogen-targeting subunit [6].
  • The neuron-specific actin-binding protein, neurabin-I, is enriched in dendritic spines, and tethers PP1 to actin-rich postsynaptic density to regulate morphology and maturation of spines [4].

Other interactions of PPP1R9A


Analytical, diagnostic and therapeutic context of PPP1R9A

  • Immunofluorescence microscopic analysis revealed that neurabin was highly concentrated in the synapse of the developed neurons [1].
  • Neurabin I interacted with PP1alpha in an overlay assay, in yeast two-hybrid interaction analysis, and in coprecipitation and co-immunoprecipitation experiments [8].


  1. Neurabin: a novel neural tissue-specific actin filament-binding protein involved in neurite formation. Nakanishi, H., Obaishi, H., Satoh, A., Wada, M., Mandai, K., Satoh, K., Nishioka, H., Matsuura, Y., Mizoguchi, A., Takai, Y. J. Cell Biol. (1997) [Pubmed]
  2. Targeting protein phosphatase 1 (PP1) to the actin cytoskeleton: the neurabin I/PP1 complex regulates cell morphology. Oliver, C.J., Terry-Lorenzo, R.T., Elliott, E., Bloomer, W.A., Li, S., Brautigan, D.L., Colbran, R.J., Shenolikar, S. Mol. Cell. Biol. (2002) [Pubmed]
  3. Direct interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin. Stephens, D.J., Banting, G. J. Biol. Chem. (1999) [Pubmed]
  4. Actin-associated neurabin-protein phosphatase-1 complex regulates hippocampal plasticity. Hu, X.D., Huang, Q., Roadcap, D.W., Shenolikar, S.S., Xia, H. J. Neurochem. (2006) [Pubmed]
  5. Genomic imprinting of PPP1R9A encoding neurabin I in skeletal muscle and extra-embryonic tissues. Nakabayashi, K., Makino, S., Minagawa, S., Smith, A.C., Bamforth, J.S., Stanier, P., Preece, M., Parker-Katiraee, L., Paton, T., Oshimura, M., Mill, P., Yoshikawa, Y., Hui, C.C., Monk, D., Moore, G.E., Scherer, S.W. J. Med. Genet. (2004) [Pubmed]
  6. Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators. Gibbons, J.A., Weiser, D.C., Shenolikar, S. J. Biol. Chem. (2005) [Pubmed]
  7. MAGI-3 regulates LPA-induced activation of Erk and RhoA. Zhang, H., Wang, D., Sun, H., Hall, R.A., Yun, C.C. Cell. Signal. (2007) [Pubmed]
  8. Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation. McAvoy, T., Allen, P.B., Obaishi, H., Nakanishi, H., Takai, Y., Greengard, P., Nairn, A.C., Hemmings, H.C. Biochemistry (1999) [Pubmed]
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