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Gene Review

ABI2  -  abl-interactor 2

Homo sapiens

Synonyms: ABI-2, ABI2B, AIP-1, ARGBPIA, Abelson interactor 2, ...
 
 
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Disease relevance of ABI2

  • Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding [1].
  • The genetic variability within PT/SAP, LYP and LXXLF HIV-1 P6gag motifs, required for the binding to Tsg101 and AIP1 cellular host proteins during viral budding, was examined in 122 HIV-infected subjects [2].
  • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding [3].
  • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1 [4].
  • BACKGROUND: Abelson (Abl) interactor 2 (Abi-2) has been considered as a key regulator of cell/tissue structural organization and is differentially expressed in leiomyomas [5].
 

High impact information on ABI2

  • Abi-2 is a novel protein that contains an SH3 domain and proline-rich sequences critical for binding to c-Abl [6].
  • We show that Abi-2 is a substrate for the c-Abl tyrosine kinase [6].
  • The cooperative activities of cofilin, coronin, and Aip1 should provide a biochemical basis for understanding how actin filaments can grow in some places in the cell while shrinking in others [4].
  • By biochemical fractionation, we identify Aip1 and coronin as two proteins present in thymus extract that facilitate the cofilin-mediated disassembly of Listeria comet tails [4].
  • Thus, ABI1 and ABI2 seem to control fibrillin expression that is involved in mediating ABA-induced photoprotection [7].
 

Biological context of ABI2

  • ABI2-deficient mice exhibit defective cell migration, aberrant dendritic spine morphogenesis, and deficits in learning and memory [8].
  • Homozygous deletion of murine abi2 produced abnormal phenotypes in the eye and brain, the tissues with the highest Abi2 expression [8].
  • The characterisation of type 2C protein phosphatases, ABI1 and ABI2, implicates negative control and redundant action on the signal pathway of this hormone [9].
  • Expression of an Abi-2 mutant protein that lacks sequences required for binding to the Abl SH3 domain but retains binding to the Abl carboxyl terminus activates the transforming capacity of c-Abl [6].
  • ArgBP1 contains a C-terminal SH3 domain, several PEST sequences, a serine rich domain and an SH3 binding site [10].
 

Anatomical context of ABI2

  • The association of ArgBP1 with Arg in living cells was confirmed by coimmunoprecipitation in cotransfected COS cells [10].
  • ArgBP1 is ubiquitously expressed as two transcripts of approximately 2.2 kb and approximately 8 kb with highest levels in brain, heart and testis [10].
  • These findings support a role for Abi2 in the regulation of cytoskeletal dynamics at adherens junctions and dendritic spines, which is critical for intercellular connectivity, cell morphogenesis, and cognitive functions [8].
  • Endogenous SETA and AIP1 proteins showed similar patterns of staining in primary rat astrocytes [11].
  • The expression of Abl interactor 2 in leiomyoma and myometrium and regulation by GnRH analogue and transforming growth factor-beta [5].
 

Associations of ABI2 with chemical compounds

  • Analysis of the mechanism of association indicated that the ArgBP1 SH3 domain binds to a C-terminal Arg SH3-binding site, and that an N-terminal ArgBP1 proline-rich sequence binds to the Arg SH3 domain [10].
  • The drug regimens consisted of single dose of albendazole 400 mg (A1, n=34), 3 days of albendazole 400 mg daily (A3, n=34), 5 days of albendazole 400 mg daily (A5, n=35), single dose of albendazole 400 mg plus praziquantel 40 mg/kg (AIP1, n=34), and 3 days of albendazole 400 mg plus praziquantel 40 mg/kg daily (A3P3, n=36) [12].
 

Other interactions of ABI2

  • In search of a function for the E3B1/Abi2/Argbp1/NESH family (Review) [13].
  • An E3B1/Abi2/Argbp1/NESH protein family has recently emerged from analysis of the sequence and structural similarities [13].
  • In line with the mutational analysis, overexpression of dominant negative (DN) mutants and wild-type TSG101 but not the DN mutant of AIP-1/ALIX reduced PFV particle release and infectivity [14].
  • ArgBP1 may be the key protein, which accounts for the physiological function of ADAM19 [15].
  • The similarity of the ArgBP1 expression pattern and subcellular localization to those of Arg and the potential for a highly specific and potentially strong association mediated by two pairs of SH3 domain/proline-rich motif interactions, suggest that ArgBP1 is likely to be a regulator and/or effector of Arg function [10].
 

Analytical, diagnostic and therapeutic context of ABI2

References

  1. Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding. Chen, C., Vincent, O., Jin, J., Weisz, O.A., Montelaro, R.C. J. Biol. Chem. (2005) [Pubmed]
  2. Variability in the P6gag domains of HIV-1 involved in viral budding. Holguín, A., Alvarez, A., Soriano, V. AIDS (2006) [Pubmed]
  3. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Strack, B., Calistri, A., Craig, S., Popova, E., Göttlinger, H.G. Cell (2003) [Pubmed]
  4. Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1. Brieher, W.M., Kueh, H.Y., Ballif, B.A., Mitchison, T.J. J. Cell Biol. (2006) [Pubmed]
  5. The expression of Abl interactor 2 in leiomyoma and myometrium and regulation by GnRH analogue and transforming growth factor-beta. Luo, X., Levens, E., Williams, R.S., Chegini, N. Hum. Reprod. (2006) [Pubmed]
  6. Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity. Dai, Z., Pendergast, A.M. Genes Dev. (1995) [Pubmed]
  7. Fibrillin expression is regulated by abscisic acid response regulators and is involved in abscisic acid-mediated photoprotection. Yang, Y., Sulpice, R., Himmelbach, A., Meinhard, M., Christmann, A., Grill, E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  8. ABI2-deficient mice exhibit defective cell migration, aberrant dendritic spine morphogenesis, and deficits in learning and memory. Grove, M., Demyanenko, G., Echarri, A., Zipfel, P.A., Quiroz, M.E., Rodriguiz, R.M., Playford, M., Martensen, S.A., Robinson, M.R., Wetsel, W.C., Maness, P.F., Pendergast, A.M. Mol. Cell. Biol. (2004) [Pubmed]
  9. ABA signal transduction. Grill, E., Himmelbach, A. Curr. Opin. Plant Biol. (1998) [Pubmed]
  10. Identification of ArgBP1, an Arg protein tyrosine kinase binding protein that is the human homologue of a CNS-specific Xenopus gene. Wang, B., Mysliwiec, T., Krainc, D., Jensen, R.A., Sonoda, G., Testa, J.R., Golemis, E.A., Kruh, G.D. Oncogene (1996) [Pubmed]
  11. The glioma-associated protein SETA interacts with AIP1/Alix and ALG-2 and modulates apoptosis in astrocytes. Chen, B., Borinstein, S.C., Gillis, J., Sykes, V.W., Bogler, O. J. Biol. Chem. (2000) [Pubmed]
  12. A comparative trial of albendazole alone versus combination of albendazole and praziquantel for treatment of Trichuris trichiura infection. Sirivichayakul, C., Pojjaroen-anant, C., Wisetsing, P., Chanthavanich, P., Praevanit, R., Limkittikul, K., Pengsaa, K. Southeast Asian J. Trop. Med. Public Health (2001) [Pubmed]
  13. In search of a function for the E3B1/Abi2/Argbp1/NESH family (Review). Ichigotani, Y., Fujii, K., Hamaguchi, M., Matsuda, S. Int. J. Mol. Med. (2002) [Pubmed]
  14. Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity. Stange, A., Mannigel, I., Peters, K., Heinkelein, M., Stanke, N., Cartellieri, M., Göttlinger, H., Rethwilm, A., Zentgraf, H., Lindemann, D. J. Virol. (2005) [Pubmed]
  15. Screen and identification of proteins interacting with ADAM19 cytoplasmic tail. Huang, L., Feng, L., Yang, L., Zhou, W., Zhao, S., Li, C. Mol. Biol. Rep. (2002) [Pubmed]
  16. A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities. Clark, M.G., Teply, J., Haarer, B.K., Viggiano, S.C., Sept, D., Amberg, D.C. Mol. Biol. Cell (2006) [Pubmed]
 
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