The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Pp1-13C  -  Protein phosphatase 1 at 13C

Drosophila melanogaster

Synonyms: 13C, CG9156, DmPp1-13C, Dmel\CG9156, PP1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Pp1-13C

  • Together these data suggest that PP1c is targeted to Dpp receptor complexes by Sara, where it acts as a negative regulator of Dpp signaling by affecting the phosphorylation state of the type I receptor [1].
  • KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1) [2].
  • In contrast, expression of transgenes encoding the Bif F995A mutant, which disrupts binding to PP1, was unable to rescue any aspect of the bif phenotype [3].
  • The gene bifocal (bif), required for photoreceptor morphogenesis in the Drosophila compound eye, encodes a protein that is shown to interact with protein phosphatase 1 (PP1) using the yeast two-hybrid system [3].
  • Type 1 serine/threonine protein phosphatases (PP1) are important regulators of many cellular and developmental processes, including glycogen metabolism, muscle contraction, and the cell cycle [1] [2] [3] [4] [5] [4].

Biological context of Pp1-13C

  • Phosphatase inhibitor-2 (I-2) is a mammalian phosphoprotein that binds to the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1c) and inhibits its activity in vitro [5].
  • Drosophila is an excellent model organism in which to characterize the role of PP1 catalytic and regulatory subunits, because it combines molecular and biochemical approaches with powerful genetics, in a well-characterized animal model [6].
  • Regulatory subunits of PP1 provide the key to understanding the role of PP1, as they are responsible for directing PP1c to different intracellular locations and/or affecting their activity or substrate specificity [6].
  • These results suggest that scapinin is a putative regulatory subunit of PP1 and is involved in transformed or immature phenotypes of HL-60 cells [7].
  • We have isolated human cDNA for a novel type 1 protein phosphatase (PP1) inhibitory protein, named inhibitor-4 (I-4), from a cDNA library of germ cell tumors [8].

Anatomical context of Pp1-13C


Associations of Pp1-13C with chemical compounds

  • Recombinant PP1c differs from native PP1c in several biochemical criteria, including the requirement for Mn(2+), sensitivity to vanadate, and p-nitrophenyl phosphate (pNPP) phosphatase activity [5].
  • PP1 (protein phosphatase-1), a major class of serine/threonine protein phosphatase, is found at many sites on Drosophila polytene chromosomes where it is involved in controlling gene expression and chromatin structure [10].

Analytical, diagnostic and therapeutic context of Pp1-13C


  1. PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster. Bennett, D., Alphey, L. Nat. Genet. (2002) [Pubmed]
  2. KLP38B: a mitotic kinesin-related protein that binds PP1. Alphey, L., Parker, L., Hawcroft, G., Guo, Y., Kaiser, K., Morgan, G. J. Cell Biol. (1997) [Pubmed]
  3. Interaction with protein phosphatase 1 Is essential for bifocal function during the morphogenesis of the Drosophila compound eye. Helps, N.R., Cohen, P.T., Bahri, S.M., Chia, W., Babu, K. Mol. Cell. Biol. (2001) [Pubmed]
  4. Protein phosphatase 1beta is required for the maintenance of muscle attachments. Raghavan, S., Williams, I., Aslam, H., Thomas, D., Szöor, B., Morgan, G., Gross, S., Turner, J., Fernandes, J., VijayRaghavan, K., Alphey, L. Curr. Biol. (2000) [Pubmed]
  5. The chaperone-like properties of mammalian inhibitor-2 are conserved in a Drosophila homologue. Bennett, D., Szöor, B., Alphey, L. Biochemistry (1999) [Pubmed]
  6. Yeast Two-Hybrid Screens to Identify Drosophila PP1-Binding Proteins. Bennett, D., Alphey, L. Methods Mol. Biol. (2006) [Pubmed]
  7. Scapinin, a putative protein phosphatase-1 regulatory subunit associated with the nuclear nonchromatin structure. Sagara, J., Higuchi, T., Hattori, Y., Moriya, M., Sarvotham, H., Shima, H., Shirato, H., Kikuchi, K., Taniguchi, S. J. Biol. Chem. (2003) [Pubmed]
  8. Identification and characterization of a novel protein inhibitor of type 1 protein phosphatase. Shirato, H., Shima, H., Sakashita, G., Nakano, T., Ito, M., Lee, E.Y., Kikuchi, K. Biochemistry (2000) [Pubmed]
  9. Bifocal and PP1 interaction regulates targeting of the R-cell growth cone in Drosophila. Babu, K., Bahri, S., Alphey, L., Chia, W. Dev. Biol. (2005) [Pubmed]
  10. Transcriptional control by chromosome-associated protein phosphatase-1. Bennett, D. Biochem. Soc. Trans. (2005) [Pubmed]
  11. Trithorax interacts with type 1 serine/threonine protein phosphatase in Drosophila. Rudenko, A., Bennett, D., Alphey, L. EMBO Rep. (2003) [Pubmed]
WikiGenes - Universities