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Ap2a2  -  adaptor-related protein complex 2, alpha 2...

Mus musculus

Synonyms: 100 kDa coated vesicle protein C, 2410074K14Rik, AF006990, AP-2 complex subunit alpha-2, AW146353, ...
 
 
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Disease relevance of Ap2a2

  • Interaction of ribosomal proteins L25 from yeast and EL23 from E. coli with yeast 26S and mouse 28S rRNA [1].
 

High impact information on Ap2a2

 

Biological context of Ap2a2

  • These results, taken together, suggest that TS accelerates osteoblast differentiation and osteogenesis, possibly through the induction of the alpha-adaptin C expression and consequent activation of receptor-mediated endocytosis [4].
  • Binding experiments using synthetic mouse 28S rRNA fragments showed that neither EL23 nor L25 interact with the structural equivalent of their respective cognate binding sites present in this mammalian rRNA [1].
  • To examine the cellular localization of ALADIN mutants causing triple A syndrome, we investigated nine different ALADIN-mutants: 2 nonsense (W84X, Q456X), 2 frameshift (F157fsX171, G397fsX414) and 5 point mutations (Q15K, L25P, H160R, S263P, L381R) by transfection experiments with green fluorescence protein [5].
 

Analytical, diagnostic and therapeutic context of Ap2a2

References

  1. Interaction of ribosomal proteins L25 from yeast and EL23 from E. coli with yeast 26S and mouse 28S rRNA. el-Baradi, T.T., de Regt, V.C., Planta, R.J., Nierhaus, K.H., Raué, H.A. Biochimie (1987) [Pubmed]
  2. Rat mast cell lines bind to the vascular cell adhesion molecule-1 (VCAM-1) and the mucosal addressin cell adhesion molecule-1 (MAdCAM-1). Palecanda, A., Briskin, M.J., Issekutz, T.B. J. Immunol. (1997) [Pubmed]
  3. Ribosomal protein L25 from Trypanosoma brucei: phylogeny and molecular co-evolution of an rRNA-binding protein and its rRNA binding site. Metzenberg, S., Joblet, C., Verspieren, P., Agabian, N. Nucleic Acids Res. (1993) [Pubmed]
  4. Tensile stress induces alpha-adaptin C production in mouse calvariae in an organ culture: possible involvement of endocytosis in mechanical stress-stimulated osteoblast differentiation. Shimomura, J., Ishibashi, O., Ikegame, M., Yoshizawa, T., Ejiri, S., Noda, T., Kawashima, H. J. Cell. Physiol. (2003) [Pubmed]
  5. The triple A syndrome is due to mutations in ALADIN, a novel member of the nuclear pore complex. Huebner, A., Kaindl, A.M., Knobeloch, K.P., Petzold, H., Mann, P., Koehler, K. Endocr. Res. (2004) [Pubmed]
 
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