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ARL2  -  ADP-ribosylation factor-like 2

Homo sapiens

Synonyms: ADP-ribosylation factor-like protein 2, ARFL2
 
 
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High impact information on ARL2

  • Somewhat paradoxically, no phenotypes were observed Arl2 expression was knocked down or Arl3 activity was increased in HeLa cells [1].
  • We conclude that Arl2 and Arl3 have related but distinct roles at centrosomes and in regulating microtubule-dependent processes [1].
  • In contrast, an excess of Arl2 activity, achieved by expression of the [Q70L]Arl2 mutant, caused the loss of microtubules and cell cycle arrest in M phase [1].
  • Recent results revealed that a portion of cellular Arl2 and its binding partner, BART, localize to mitochondria [2].
  • Like ARL2 and -3, recombinant hARL4 did not enhance cholera toxin-catalyzed auto-ADP-ribosylation [3].
 

Biological context of ARL2

  • Two-hybrid screens of human cDNA libraries with dominant active mutants of human ARL1, ARL2, and ARL3 identified eight different but overlapping sets of binding partners [4].
 

Associations of ARL2 with chemical compounds

  • This chapter describes methods for preparing recombinant Arl2, loading different radiolabeled guanine nucleotides onto the GTPase, identifying high-affinity Arl2 binding proteins, and assaying Arl2 GTPase activating proteins (GAPs) [5].
 

Analytical, diagnostic and therapeutic context of ARL2

  • Because approximately 90% of cellular Arl2 is cytosolic, we investigated properties of the soluble protein and found that it is stably bound in a complex that migrates in gel filtration medium with a predicted molecular mass of approximately 300 kDa [2].

References

  1. Arl2 and Arl3 Regulate Different Microtubule-dependent Processes. Zhou, C., Cunningham, L., Marcus, A.I., Li, Y., Kahn, R.A. Mol. Biol. Cell (2006) [Pubmed]
  2. Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A. Shern, J.F., Sharer, J.D., Pallas, D.C., Bartolini, F., Cowan, N.J., Reed, M.S., Pohl, J., Kahn, R.A. J. Biol. Chem. (2003) [Pubmed]
  3. ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli. Lin, C.Y., Huang, P.H., Liao, W.L., Cheng, H.J., Huang, C.F., Kuo, J.C., Patton, W.A., Massenburg, D., Moss, J., Lee, F.J. J. Biol. Chem. (2000) [Pubmed]
  4. ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins. Van Valkenburgh, H., Shern, J.F., Sharer, J.D., Zhu, X., Kahn, R.A. J. Biol. Chem. (2001) [Pubmed]
  5. Assays used in the analysis of Arl2 and its binding partners. Bowzard, J.B., Sharer, J.D., Kahn, R.A. Meth. Enzymol. (2005) [Pubmed]
 
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