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Gene Review

ARFIP2  -  ADP-ribosylation factor interacting protein 2

Homo sapiens

Synonyms: ADP-ribosylation factor-interacting protein 2, Arfaptin-2, POR1, Partner of RAC1, Protein POR1
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Disease relevance of ARFIP2


High impact information on ARFIP2

  • A second mutant, RACV12L37 (with leucine substituted at position 37), which bound PAK but not POR1, induced JNK activation but was defective in inducing membrane ruffling and transformation [3].
  • Furthermore, we observed that ARF6 interacts directly with POR1 and that this interaction was GTP dependent [4].
  • A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements [4].
  • Truncated versions of POR1 inhibit the induction of membrane ruffling by an activated mutant of Rac1, V12Rac1, in quiescent rat embryonic fibroblast REF52 cells [5].
  • Arfaptin 2, found in the same two-hybrid screen as arfaptin 1, is 60% identical in amino acid sequence and may or may not have an analogous function [6].

Biological context of ARFIP2

  • Thus, overexpression of full-length POR1 diminished K(+)-stimulated exocytosis, and a point mutation in the effector domain of Rac1(V12) that prevents the interaction with POR1 abolished the inhibitory effect of the GTPase [7].

Anatomical context of ARFIP2

  • The mitochondria are much more attacked by the lipophilic POR10 than by the hydrophilic POR1 and TPPS [8].

Physical interactions of ARFIP2

  • Assays and properties of arfaptin 2 binding to Rac1 and ADP-ribosylation factors (Arfs) [9].

Other interactions of ARFIP2

  • Arfaptin 2 was also ubiquitously expressed and bound to the GTP-, but not GDP-liganded form of class I ARFs, especially ARF1 [10].
  • Based on our observation, we propose that arfaptin 2 is a target for GDP-Rac1 and for GTP-Arf1, and is involved in interactions between the Rac1 and Arfs signaling pathways [9].
  • A synergistic effect between POR1 and ARF6 for the induction of actin polymerization was detected [4].

Analytical, diagnostic and therapeutic context of ARFIP2

  • Cytotoxic and phototoxic effects were studied by means of electron microscopy and respiratory activity and compared with the effects of the hydrophilic cationic hin tetraiodide (POR1) and the anionic,23H-porp hin (TPPS) [8].
  • Positive rate of lavage cytodiagnosis was significantly higher in por2 (38.9%), than that in por1 (9.1%) [1].


  1. Clinicopathological analysis of poorly differentiated adenocarcinoma of the stomach. Imada, T., Rino, Y., Takahashi, M., Hatori, S., Shinozawa, M., Tanaka, J., Suzuki, M., Amano, T., Kondo, J. Hepatogastroenterology (1999) [Pubmed]
  2. Beta-chemokine, macrophage inflammatory protein-1beta (MIP-1beta), is highly expressed in diffuse type human gastric cancers. Saito, S., Kitayama, J., Jin, Z.X., Tsuno, N., Kaisaki, S., Seto, Y., Nagawa, H. J. Exp. Clin. Cancer Res. (2003) [Pubmed]
  3. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Joneson, T., McDonough, M., Bar-Sagi, D., Van Aelst, L. Science (1996) [Pubmed]
  4. A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. D'Souza-Schorey, C., Boshans, R.L., McDonough, M., Stahl, P.D., Van Aelst, L. EMBO J. (1997) [Pubmed]
  5. Identification of a novel Rac1-interacting protein involved in membrane ruffling. Van Aelst, L., Joneson, T., Bar-Sagi, D. EMBO J. (1996) [Pubmed]
  6. Effects of arfaptin 1 on guanine nucleotide-dependent activation of phospholipase D and cholera toxin by ADP-ribosylation factor. Tsai, S.C., Adamik, R., Hong, J.X., Moss, J., Vaughan, M., Kanoh, H., Exton, J.H. J. Biol. Chem. (1998) [Pubmed]
  7. Involvement of Rho GTPases and their effectors in the secretory process of PC12 cells. Frantz, C., Coppola, T., Regazzi, R. Exp. Cell Res. (2002) [Pubmed]
  8. Selective photosensitization of mitochondria by the lipophilic cationic porphyrin POR10. Cernay, T., Zimmermann, H.W. J. Photochem. Photobiol. B, Biol. (1996) [Pubmed]
  9. Assays and properties of arfaptin 2 binding to Rac1 and ADP-ribosylation factors (Arfs). Shin, O.H., Exton, J.H. Meth. Enzymol. (2005) [Pubmed]
  10. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. Kanoh, H., Williger, B.T., Exton, J.H. J. Biol. Chem. (1997) [Pubmed]
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