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Pag1  -  phosphoprotein membrane anchor with...

Rattus norvegicus

Synonyms: Cbp, Csk-binding protein, Pag, Phosphoprotein associated with glycosphingolipid-enriched microdomains 1, Transmembrane phosphoprotein Cbp
 
 
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High impact information on Cbp

  • In the plasma membrane Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signalling [1].
  • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases [1].
  • Upon SFK activation induced by epidermal growth factor stimulation, fluorescent resonance energy transfer (FRET) response was detected transiently at membrane ruffles in COS1 cells co-expressing CFP-Csk and Cbp-YFP and in cells expressing a single-molecule FRET indicator consisting of CskSH2 and Cbp [2].
  • Cutting Edge: Transmembrane phosphoprotein Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched microdomains as a negative feedback regulator of mast cell signaling through the FcepsilonRI [3].
  • In contrast, Pag inhibits tumorigenesis by c-Myc-overexpressing fibroblasts and causes a broad but selective loss of c-Myc target gene regulation [4].
 

Biological context of Cbp

  • We now show that Pag promotes increased cell size and confers a proapoptotic phenotype, two hallmark features of ectopic c-Myc overexpression [4].
 

Anatomical context of Cbp

  • Pag-1 is expressed on bone marrow-derived cells, since peritoneal cells from lethally irradiated MAXX rats that were reconstituted with bone marrow cells from BN donors reacted with MAXX anti-BN sera, whereas peritoneal cells from BN rats reconstituted with MAXX bone marrow did not [5].
  • Pag-1 appears to be absent in the kidney, since absorption of MAXX anti-BN sera with BN kidney homogenates did not remove the reactivity against Pag-1, and antisera raised against BN peritoneal cells did not bind with the renal endothelium [5].
 

Associations of Cbp with chemical compounds

  • Csk was also activated by a phosphopeptide containing the tyrosine in Cbp that binds to Csk (Tyr-314) [6].
 

Enzymatic interactions of Cbp

  • Csk and phosphorylated Cbp were co-purified as a large protein complex consisting of at least four Csk.Cbp units [6].
 

Other interactions of Cbp

  • The Cbp-mediated relocation of Csk to the membrane may play a role in turning off the signaling events initiated by SFKs [6].

References

  1. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Kawabuchi, M., Satomi, Y., Takao, T., Shimonishi, Y., Nada, S., Nagai, K., Tarakhovsky, A., Okada, M. Nature (2000) [Pubmed]
  2. Mechanism of Csk-mediated down-regulation of Src family tyrosine kinases in epidermal growth factor signaling. Matsuoka, H., Nada, S., Okada, M. J. Biol. Chem. (2004) [Pubmed]
  3. Cutting Edge: Transmembrane phosphoprotein Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched microdomains as a negative feedback regulator of mast cell signaling through the FcepsilonRI. Ohtake, H., Ichikawa, N., Okada, M., Yamashita, T. J. Immunol. (2002) [Pubmed]
  4. Pag, a putative tumor suppressor, interacts with the Myc Box II domain of c-Myc and selectively alters its biological function and target gene expression. Mu, Z.M., Yin, X.Y., Prochownik, E.V. J. Biol. Chem. (2002) [Pubmed]
  5. A novel alloantigen on rat macrophages and granulocytes. Blankert, J.J., Muizert, Y., Olijans, P.J., van Es, L.A., Paul, L.C. Immunogenetics (1985) [Pubmed]
  6. Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk. Takeuchi, S., Takayama, Y., Ogawa, A., Tamura, K., Okada, M. J. Biol. Chem. (2000) [Pubmed]
 
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