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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 5.10.15.20-tetrakis(1-methylpyridinium-4-yl)-21H.23H-porp hin tetraiodide (POR1) and the anionic 5.10.15.20-tetrakis(1-sulphophen-4-yl)-21H,23H-porp hin (TPPS) [8].
  • Positive rate of lavage cytodiagnosis was significantly higher in por2 (38.9%), than that in por1 (9.1%) [1].

References

  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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