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ARL6IP1  -  ADP-ribosylation factor-like 6 interacting...

Homo sapiens

Synonyms: ADP-ribosylation factor-like protein 6-interacting protein 1, AIP1, ARL-6-interacting protein 1, ARL6IP, ARMER, ...
 
 
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Disease relevance of ARL6IP1

  • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1 [1].
  • Interactions between Nef and AIP1 proliferate multivesicular bodies and facilitate egress of HIV-1 [2].
 

High impact information on ARL6IP1

  • 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 [1].
  • 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 [1].
  • To better describe the mechanisms and biological consequences of Aip1p activities, we undertook an extensive mutagenesis of AIP1 aimed at disrupting and mapping Aip1p interactions [3].
  • Site-directed mutagenesis suggested that Aip1p has two actin binding sites, the primary actin binding site lies on the edge of its N-terminal beta-propeller and a secondary actin binding site lies in a comparable location on its C-terminal beta-propeller [3].
  • Biochemical, genetic, and cell biological analyses confirmed that the actin binding- and cofilin binding-specific mutants are functionally defective, whereas the genetic analyses further suggested a role for Aip1p in an early, internalization step of endocytosis [3].
 

Biological context of ARL6IP1

  • A complementary, unbiased molecular modeling approach was used to derive putative structures for the Aip1p-cofilin complex, the most stable of which is completely consistent with the mutagenesis data [3].
  • The two important functional motifs within NC, the zinc-finger motifs, were highly conserved in most of the sequences, as were the gag p6 Vpr binding, AIP1 and late binding domains [4].
 

Anatomical context of ARL6IP1

 

Associations of ARL6IP1 with chemical compounds

  • In five experiments, T3 (60 nM, 18-hr incubation) consistently repressed AIP-1, while aldosterone-dependent sodium transport (late response) was significantly inhibited, as previously described [6].
 

Analytical, diagnostic and therapeutic context of ARL6IP1

  • A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities [3].

References

  1. 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]
  2. Interactions between Nef and AIP1 proliferate multivesicular bodies and facilitate egress of HIV-1. Costa, L.J., Chen, N., Lopes, A., Aguiar, R.S., Tanuri, A., Plemenitas, A., Peterlin, B.M. Retrovirology (2006) [Pubmed]
  3. 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]
  4. Molecular characterization of the HIV-1 gag nucleocapsid gene associated with vertical transmission. Wellensiek, B.P., Sundaravaradan, V., Ramakrishnan, R., Ahmad, N. Retrovirology (2006) [Pubmed]
  5. Characterization, chromosomal localization, and expression during hematopoietic differentiation of the gene encoding Arl6ip, ADP-ribosylation-like factor-6 interacting protein (ARL6). Pettersson, M., Bessonova, M., Gu, H.F., Groop, L.C., Jönsson, J.I. Genomics (2000) [Pubmed]
  6. Thyroid hormone antagonizes an aldosterone-induced protein: a candidate mediator for the late mineralocorticoid response. Truscello, A., Gäggeler, H.P., Rossier, B.C. J. Membr. Biol. (1986) [Pubmed]
 
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