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Gene Review

PAIP2  -  poly(A) binding protein interacting protein 2

Homo sapiens

Synonyms: HSPC218, PABP-interacting protein 2, PAIP-2, PAIP2A, Poly(A)-binding protein-interacting protein 2, ...
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Disease relevance of PAIP2

  • Our data suggest that, in contrast to PAIP2 protein levels, which are unrelated to tumour prognosis, VEGF-A expression could serve as a prognostic marker in head and neck cancer and may be helpful for targeted therapies [1].
  • Furthermore, one of the six Ags, a novel Ag homologous to HSPC218, showed restricted expression in normal testis, suggesting that it belongs to the cancer-testis Ag family [2].

High impact information on PAIP2


Biological context of PAIP2


Associations of PAIP2 with chemical compounds


Regulatory relationships of PAIP2

  • This was confirmed by experiments where PABP was inactivated with poly(rA) or Paip2, and the effect of both treatments was reversed by addition of recombinant PABP [9].

Other interactions of PAIP2

  • Hence, PAIP2 appears to be a crucial regulator of VEGF mRNA and as a consequence, any variation in its expression could modulate angiogenesis [6].
  • The PABC domain from human PABP interacts with the proteins PAIP1, PAIP2 and RF3 via its PAM2 motifs [10].
  • This domain recruits a series of translation factors including poly(A)-interacting proteins (Paip1 and Paip2) and release factor 3 (RF3/GSPT) to the initiation complex on mRNA [11].


  1. Vascular endothelial growth factor-A and Poly(A) binding protein-interacting protein 2 expression in human head and neck carcinomas: correlation and prognostic significance. Onesto, C., Hannoun-Lévi, J.M., Chamorey, E., Formento, J.L., Ramaioli, A., Pagès, G. Br. J. Cancer (2006) [Pubmed]
  2. A panel of candidate tumor antigens in colorectal cancer revealed by the serological selection of a phage displayed cDNA expression library. Somers, V.A., Brandwijk, R.J., Joosten, B., Moerkerk, P.T., Arends, J.W., Menheere, P., Pieterse, W.O., Claessen, A., Scheper, R.J., Hoogenboom, H.R., Hufton, S.E. J. Immunol. (2002) [Pubmed]
  3. Enhancement of IRES-mediated translation of the c-myc and BiP mRNAs by the poly(A) tail is independent of intact eIF4G and PABP. Thoma, C., Bergamini, G., Galy, B., Hundsdoerfer, P., Hentze, M.W. Mol. Cell (2004) [Pubmed]
  4. Poly(A) binding protein (PABP) homeostasis is mediated by the stability of its inhibitor, Paip2. Yoshida, M., Yoshida, K., Kozlov, G., Lim, N.S., De Crescenzo, G., Pang, Z., Berlanga, J.J., Kahvejian, A., Gehring, K., Wing, S.S., Sonenberg, N. EMBO J. (2006) [Pubmed]
  5. Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase. Kozlov, G., De Crescenzo, G., Lim, N.S., Siddiqui, N., Fantus, D., Kahvejian, A., Trempe, J.F., Elias, D., Ekiel, I., Sonenberg, N., O'Connor-McCourt, M., Gehring, K. EMBO J. (2004) [Pubmed]
  6. Poly(A)-binding protein-interacting protein 2, a strong regulator of vascular endothelial growth factor mRNA. Onesto, C., Berra, E., Grépin, R., Pagès, G. J. Biol. Chem. (2004) [Pubmed]
  7. Dual interactions of the translational repressor Paip2 with poly(A) binding protein. Khaleghpour, K., Kahvejian, A., De Crescenzo, G., Roy, G., Svitkin, Y.V., Imataka, H., O'Connor-McCourt, M., Sonenberg, N. Mol. Cell. Biol. (2001) [Pubmed]
  8. Fructose modulates GLUT5 mRNA stability in differentiated Caco-2 cells: role of cAMP-signalling pathway and PABP (polyadenylated-binding protein)-interacting protein (Paip) 2. Gouyon, F., Onesto, C., Dalet, V., Pages, G., Leturque, A., Brot-Laroche, E. Biochem. J. (2003) [Pubmed]
  9. mRNA with a <20-nt poly(A) tail imparted by the poly(A)-limiting element is translated as efficiently in vivo as long poly(A) mRNA. Peng, J., Schoenberg, D.R. RNA (2005) [Pubmed]
  10. Four distinct classes of proteins as interaction partners of the PABC domain of Arabidopsis thaliana Poly(A)-binding proteins. Bravo, J., Aguilar-Henonin, L., Olmedo, G., Guzmán, P. Mol. Genet. Genomics (2005) [Pubmed]
  11. Solution structure of the C-terminal domain from poly(A)-binding protein in Trypanosoma cruzi: a vegetal PABC domain. Siddiqui, N., Kozlov, G., D'Orso, I., Trempe, J.F., Gehring, K. Protein Sci. (2003) [Pubmed]
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